subject:(peroxidase)

Oregon State University

1. Jiang, Shu. Selective oxidation of biological matrices for subsequent peroxidase and peroxidase-based quantitative analyses.

Degree: MS, Food Science and Technology, 2014, Oregon State University

URL: http://hdl.handle.net/1957/52549

► Hydrogen peroxide quantification is of broad interest due to the common use of hydrogen peroxide as an oxidizing agent in industrial processing and laboratory research.… (more)

▼ Hydrogen peroxide quantification is of broad interest due to the common use of hydrogen peroxide as an oxidizing agent in industrial processing and laboratory research. Hydrogen peroxide assays are also of general importance for biological studies aimed at understanding the role of in situ generated reactive oxygen species. In the latter scenario particularly, assays amenable to high throughput processing are needed. Peroxidase-based methods are appropriate for such applications due to the high selectivity and sensitivity of enzyme catalyzed reactions. A problem commonly encountered when using peroxidase-based methods to quantify the level of hydrogen peroxide in biological samples is assay interference due the presence of assay-modifying endogenous compounds. This type of interference has limited the applicability of peroxidase/chromophore linked assays which are commonly used elsewhere for high throughput screening (e.g., the glucose oxidase/peroxidase assay for glucose quantification). Potential mechanisms of assay interference include enzyme inhibition/inactivation, substrate competition and product modification. In the present study we addressed the different mechanisms of interference, especially product (oxidized reporter molecule) modification, using the following system: horseradish peroxidase, 2,2' azino-bis(3-ethylbenzothiazoline-6-sulphonic acid) (ABTS) and a hydrogen peroxide-containing garlic paste extract (GPE). Methods using ABTS as an appropriate reporter molecule to circumvent the interference are based on removal of confounding compounds, particularly referred to as natural antioxidants, prior to initiating the assay. Because confounding compounds interfere with the peroxidase-based assay by converting peroxidase-catalyzed ABTS oxidation product, ABTS•⁺ back to ABTS, prepared ABTS•⁺ was used to selectively oxidize, thus inactivate confounding compounds that would cause confounding in this assay. A calibration curve generated by using ABTS•⁺ treated GPE sample was not significantly different (p>0.05) from the curve obtained in the model buffer system. In contrast to a flat baseline generated by original GPE sample, the effectiveness of ABTS•⁺ treatment in hydrogen peroxide quantification in the presence of interference was proved. This assay allows one to simply determine the amount of hydrogen peroxide in a product in situ and thus avoids the need for sophisticated separation techniques. The limitation of the method is that the treatment required for removal of confounding compounds takes on the order of minutes and thus the method has the possibility of underestimating the hydrogen peroxide content in systems where such concentrations are changing on the seconds to minutes time scale. The other focus of this project was a modified assay that eliminates a source of underestimation of peroxidase activity in plant extracts. Natural reducing agents endogenous to plant materials, such as phenolic compounds and ascorbic acid, may interfere with traditional peroxidase assays by reducing the oxidized… Advisors/Committee Members: Penner, Michael H. (advisor), Tomasino, Elizabeth (committee member).

Subjects/Keywords: Peroxidase

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APA (6^th Edition):

Jiang, S. (2014). Selective oxidation of biological matrices for subsequent peroxidase and peroxidase-based quantitative analyses. (Masters Thesis). Oregon State University. Retrieved from http://hdl.handle.net/1957/52549

Chicago Manual of Style (16^th Edition):

Jiang, Shu. “Selective oxidation of biological matrices for subsequent peroxidase and peroxidase-based quantitative analyses.” 2014. Masters Thesis, Oregon State University. Accessed April 17, 2021. http://hdl.handle.net/1957/52549.

MLA Handbook (7^th Edition):

Jiang, Shu. “Selective oxidation of biological matrices for subsequent peroxidase and peroxidase-based quantitative analyses.” 2014. Web. 17 Apr 2021.

Vancouver:

Jiang S. Selective oxidation of biological matrices for subsequent peroxidase and peroxidase-based quantitative analyses. [Internet] [Masters thesis]. Oregon State University; 2014. [cited 2021 Apr 17]. Available from: http://hdl.handle.net/1957/52549.

Council of Science Editors:

Jiang S. Selective oxidation of biological matrices for subsequent peroxidase and peroxidase-based quantitative analyses. [Masters Thesis]. Oregon State University; 2014. Available from: http://hdl.handle.net/1957/52549

Oregon State University

2. Darussamin, Asril. Reactions of horseradish peroxidase with the isothiocyanates of horseradish oil.

Degree: PhD, Biochemistry and Biophysics, 1984, Oregon State University

URL: http://hdl.handle.net/1957/40969

► Horseradish peroxidase (HRP) has been investigated extensively and for many years. In spite of this it still exhibits unexplained anomalies. Among these is variation in… (more)

▼ Horseradish peroxidase (HRP) has been investigated extensively and for many years. In spite of this it still exhibits unexplained anomalies. Among these is variation in the reported number of isozymes (from 7 to 42), and reports of instability of the isozyme patterns. Since horseradish is a rich source of organic isothiocyanates (mustard oils), it seemed likely that artifactual chemical modification of the enzyme might occur during or after extraction. The present investigation demonstrates that isothiocyanates can in fact cause extensive modification of HRP without corresponding loss of catalytic activity. Incubation of HRP with isothiocyanates at alkaline pH and 4°C altered the isozyme pattern. Peroxidase activity was shifted from bands of higher p1 to bands of lower p1, some of them preexisting bands and some of them newly generated. With time, the basic "C" band, initially the principal isozyme, virtually disappeared, and enzyme activity shifted to bands of lower pr. These were discrete bands, presumably formed by stepwise blocking of successive amino groups. Modification of HRP was found to be dependent on pH, reaction time, and isothiocyanate concentration. Amino acid analysis showed loss of 50 % of the lysine residues after reaction of HRP with allylisothiocyanate at pH 10. Reaction of phenyl- (¹⁴C)isothiocyanate with HRP at pH 10 resulted in an average of five phenylisothiocyanates incorporated per enzyme molecule. Autoradiography showed four radioactive HRP bands , corresponding to a shift of enzyme activity into these bands. Incubation of HRP with allylisothiocyanate in the presence of L-lysine at pH 10 showed little protective effect of the lysine, although the concentration of lysine was 800 times the enzyme concentration. This suggested that hydrophobic sites that bind isothiocyanates to the enzyme surface enhance the reaction of the isothiocyanates with the enzyme. Extraction of HRP from horseradish roots in the presence of adsorbent pclystyrene resulted in extracts that were colorless and odorless, in contrast to the brown color and pungent odor of untreated extracts. The initial extracts showed no difference in isozyme pattern between polystyrene-treated and untreated extracts. After ammonium sulfate precipitation, however, the polystyrene-treated extract retained the original isozyme pattern, while the untreated extract produced new bands of lower pI. Advisors/Committee Members: Loomis, W. David (advisor).

Subjects/Keywords: Peroxidase

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APA (6^th Edition):

Darussamin, A. (1984). Reactions of horseradish peroxidase with the isothiocyanates of horseradish oil. (Doctoral Dissertation). Oregon State University. Retrieved from http://hdl.handle.net/1957/40969

Chicago Manual of Style (16^th Edition):

Darussamin, Asril. “Reactions of horseradish peroxidase with the isothiocyanates of horseradish oil.” 1984. Doctoral Dissertation, Oregon State University. Accessed April 17, 2021. http://hdl.handle.net/1957/40969.

MLA Handbook (7^th Edition):

Darussamin, Asril. “Reactions of horseradish peroxidase with the isothiocyanates of horseradish oil.” 1984. Web. 17 Apr 2021.

Vancouver:

Darussamin A. Reactions of horseradish peroxidase with the isothiocyanates of horseradish oil. [Internet] [Doctoral dissertation]. Oregon State University; 1984. [cited 2021 Apr 17]. Available from: http://hdl.handle.net/1957/40969.

Council of Science Editors:

Darussamin A. Reactions of horseradish peroxidase with the isothiocyanates of horseradish oil. [Doctoral Dissertation]. Oregon State University; 1984. Available from: http://hdl.handle.net/1957/40969

Oregon State University

3. Rodriguez-Saona, Luis Enrique. Peroxidase and lipoxygenase activities and their effect on the stability of polyunsaturated fatty acids in two different varieties of sweet corn (Zea mays L.), Jubilee and GH 2684, during frozen storage.

Degree: MS, Food Science and Technology, 1993, Oregon State University

URL: http://hdl.handle.net/1957/27144

► The effect of different blanching treatments and packaging materials on the enzymatic (lipoxygenase and peroxidase) activity and fatty acid stability of two different varieties of… (more)

▼ The effect of different blanching treatments and packaging materials on the enzymatic (lipoxygenase and peroxidase) activity and fatty acid stability of two different varieties of sweet corn on the cob (Jubilee and GH 2684) was evaluated during nine months of frozen storage at -23.3°C. The initial moisture content in the kernels of the two sweet corn varieties averaged 72.5%. After nine months of frozen storage the moisture content in the kernels of corn depended greatly on the packaging material used. The ears stored in Cryovac B and E bags showed the best moisture retention (72.2% final moisture content), followed by the polyethylene bags (71.4%) while the ears stored without packaging material showed severe dehydration (70.1%). The peroxidase and lipoxygenase activities were determined using spectrophotometric assays on a crude extract obtained from liquid nitrogen powdered corn. Both unblanched varieties of sweet corn showed similar initial peroxidase specific activity and general behavior during the nine months of frozen storage. The presence of lipoxygenase isozymes with different thermal stabilities in both varieties was suggested by the higher lipoxygenase specific activity found in Jubilee after freezing and nine months of frozen storage (0.135 units/mg protein) compared with the GH 2684 variety (0.115 units/mg protein). Complete inactivation of lipoxygenase was obtained after 9 minutes steam blanching at 100°C. Peroxidase was more heat resistant showing some remaining specific activity after 9 minutes steam blanching with a complete inactivation after 15 minutes steam blanching. No regeneration of either enzyme was observed during the nine months of frozen storage suggesting a permanent disruption of the active site of both enzymes. Relative fatty acid content was determined by gas chromatographic analysis of fatty acids methyl esters. The major fatty acids present in both varieties were palmitic (14.93%), stearic (2.79%), oleic (31.54%), linoleic (46.87%) and linolenic (1.89%) acids. Good stability of the polyunsaturated fatty acids was observed during the nine months storage at -23.3°C, with autoxidation as the main mechanism responsible for the decrease in the relative percent of polyunsaturated fatty acids. Some enzymatic oxidation also occurred, decreasing the linolenic acid content. The control of the degradation of polyunsaturated fatty acids depended mostly on the frozen storage temperature (-23.3°C) and not on the oxygen permeability of the different packaging materials. The results obtained in our study suggested that blanching of the ears of sweet corn had an important effect on reducing the enzyme activity but little effect on the polyunsaturated fatty acid degradation after 9 months of storage at -23.3°C. Advisors/Committee Members: Selivonchick, Daniel P. (advisor).

Subjects/Keywords: Peroxidase

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APA (6^th Edition):

Rodriguez-Saona, L. E. (1993). Peroxidase and lipoxygenase activities and their effect on the stability of polyunsaturated fatty acids in two different varieties of sweet corn (Zea mays L.), Jubilee and GH 2684, during frozen storage. (Masters Thesis). Oregon State University. Retrieved from http://hdl.handle.net/1957/27144

Chicago Manual of Style (16^th Edition):

Rodriguez-Saona, Luis Enrique. “Peroxidase and lipoxygenase activities and their effect on the stability of polyunsaturated fatty acids in two different varieties of sweet corn (Zea mays L.), Jubilee and GH 2684, during frozen storage.” 1993. Masters Thesis, Oregon State University. Accessed April 17, 2021. http://hdl.handle.net/1957/27144.

MLA Handbook (7^th Edition):

Rodriguez-Saona, Luis Enrique. “Peroxidase and lipoxygenase activities and their effect on the stability of polyunsaturated fatty acids in two different varieties of sweet corn (Zea mays L.), Jubilee and GH 2684, during frozen storage.” 1993. Web. 17 Apr 2021.

Vancouver:

Rodriguez-Saona LE. Peroxidase and lipoxygenase activities and their effect on the stability of polyunsaturated fatty acids in two different varieties of sweet corn (Zea mays L.), Jubilee and GH 2684, during frozen storage. [Internet] [Masters thesis]. Oregon State University; 1993. [cited 2021 Apr 17]. Available from: http://hdl.handle.net/1957/27144.

Council of Science Editors:

Rodriguez-Saona LE. Peroxidase and lipoxygenase activities and their effect on the stability of polyunsaturated fatty acids in two different varieties of sweet corn (Zea mays L.), Jubilee and GH 2684, during frozen storage. [Masters Thesis]. Oregon State University; 1993. Available from: http://hdl.handle.net/1957/27144

Michigan State University

4. Liu, Edwin Chiap Henn, 1942-. The isozymic forms of peroxidase found in the horseradish plant (Armoracia lapathifolia).

Degree: PhD, Department of Biochemistry, 1971, Michigan State University

URL: http://etd.lib.msu.edu/islandora/object/etd:19802

Subjects/Keywords: Peroxidase

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APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6^th Edition):

Liu, Edwin Chiap Henn, 1. (1971). The isozymic forms of peroxidase found in the horseradish plant (Armoracia lapathifolia). (Doctoral Dissertation). Michigan State University. Retrieved from http://etd.lib.msu.edu/islandora/object/etd:19802

Chicago Manual of Style (16^th Edition):

Liu, Edwin Chiap Henn, 1942-. “The isozymic forms of peroxidase found in the horseradish plant (Armoracia lapathifolia).” 1971. Doctoral Dissertation, Michigan State University. Accessed April 17, 2021. http://etd.lib.msu.edu/islandora/object/etd:19802.

MLA Handbook (7^th Edition):

Liu, Edwin Chiap Henn, 1942-. “The isozymic forms of peroxidase found in the horseradish plant (Armoracia lapathifolia).” 1971. Web. 17 Apr 2021.

Vancouver:

Liu, Edwin Chiap Henn 1. The isozymic forms of peroxidase found in the horseradish plant (Armoracia lapathifolia). [Internet] [Doctoral dissertation]. Michigan State University; 1971. [cited 2021 Apr 17]. Available from: http://etd.lib.msu.edu/islandora/object/etd:19802.

Council of Science Editors:

Liu, Edwin Chiap Henn 1. The isozymic forms of peroxidase found in the horseradish plant (Armoracia lapathifolia). [Doctoral Dissertation]. Michigan State University; 1971. Available from: http://etd.lib.msu.edu/islandora/object/etd:19802

Michigan State University

5. Ivie, Kert F. The effect of peroxidase on model systems of lipoxidase and linoleic acid.

Degree: MS, Dept. of Food Science and Human Nutrition, 1973, Michigan State University

URL: http://etd.lib.msu.edu/islandora/object/etd:10022

Subjects/Keywords: Peroxidase

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APA (6^th Edition):

Ivie, K. F. (1973). The effect of peroxidase on model systems of lipoxidase and linoleic acid. (Masters Thesis). Michigan State University. Retrieved from http://etd.lib.msu.edu/islandora/object/etd:10022

Chicago Manual of Style (16^th Edition):

Ivie, Kert F. “The effect of peroxidase on model systems of lipoxidase and linoleic acid.” 1973. Masters Thesis, Michigan State University. Accessed April 17, 2021. http://etd.lib.msu.edu/islandora/object/etd:10022.

MLA Handbook (7^th Edition):

Ivie, Kert F. “The effect of peroxidase on model systems of lipoxidase and linoleic acid.” 1973. Web. 17 Apr 2021.

Vancouver:

Ivie KF. The effect of peroxidase on model systems of lipoxidase and linoleic acid. [Internet] [Masters thesis]. Michigan State University; 1973. [cited 2021 Apr 17]. Available from: http://etd.lib.msu.edu/islandora/object/etd:10022.

Council of Science Editors:

Ivie KF. The effect of peroxidase on model systems of lipoxidase and linoleic acid. [Masters Thesis]. Michigan State University; 1973. Available from: http://etd.lib.msu.edu/islandora/object/etd:10022

Universidade Estadual de Campinas

6. Holschuh, Heinz Johann. Isolamento, purificação e caracterização bioquimica da peroxidase de carambola (Averrhoa carambola, L.).

Degree: Faculdade de Engenharia de Alimentos; Programa de Pós-Graduação em Ciência de Alimentos, 2000, Universidade Estadual de Campinas

URL: HOLSCHUH, Heinz Johann. Isolamento, purificação e caracterização bioquimica da peroxidase de carambola (Averrhoa carambola, L.). 2000. 159p. Tese (doutorado) - Universidade Estadual de Campinas, Faculdade de Engenharia de Alimentos, Campinas, SP. Disponível em: <http://www.repositorio.unicamp.br/handle/REPOSIP/256682>. Acesso em: 26 jul. 2018. ; http://repositorio.unicamp.br/jspui/handle/REPOSIP/256682

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Orientador: Glaucia Maria Pastore

Tese (doutorado) - Universidade Estadual de Campinas, Faculdade de Engenharia de Alimentos

Made available in DSpace on 2018-07-26T12:25:32Z (GMT). No. of… (more)

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Orientador: Glaucia Maria Pastore

Tese (doutorado) - Universidade Estadual de Campinas, Faculdade de Engenharia de Alimentos

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Resumo: Peroxidases (POD, EC 1.11.7.1 doador: peróxido de hidrogênio oxidoredutase) são um grupo de isoenzimas responsabilizadas pelo surgimento de alterações da coloração natural dos alimentos e sabor desagradável; são usadas em análises de alimentos, clínicas, e em conjunto com outras enzimas, na conservação de certos alimentos. Muitas frutas como a carambola (Averhoa carambola, L.) ainda não tiveram suas peroxidases avaliadas quanto às suas propriedades bioquímicas. Esse trabalho teve como objetivo isolar, purificar e caracterizar bioquimicamente a peroxidase de carambola. A localização histoquímica da peroxidase realizou-se mergulhando fatias de carambolas verdes, verde-maturas e sobre-maduras em mistura de reação constituída de 1 % de guaiacol em tampão fosfato de potássio 0,1 M pH 6,0, e 0,1 M de peróxido de hidrogênio. A evolução do escurecimento foi acompanhada e fotografada. A localização em frutas verdes e verde-maturas restringiu-se às partes mais fibrosas: junto aos feixes vasculares que atravessam a polpa, ao talo central e gineceu e à casca. Em fatia de carambola sobre-madura a polpa adquiriu coloração do tetraguaiacol e houve extravasamento do composto colorido para o meio de reação, indicando a presença de maior quantidade de enzima solúvel. Partes de carambola, casca, polpa e talo central com gineceu foram analisadas separadamente, após extração da POD com tampão mais eficiente, fosfato de potássio 0,2 M pH 8,0. Os resultados encontrados na localização histoquímica foram confirmados. Talo central com gineceu apresentaram maior atividade por grama da parte da fruta, seguido pela casca; polpa apresentou atividade considerável. apenas em carambolas sobremaduras. Carambolas verdes renderam maior atividade POD por grama, na soma das partes. Foram testados o efeito da adição de 0,2 M de CaCI2,2% de PVP, 2% de PEG, 0,01 M de EDTA e 0,01 M de ácido L-ascórbico, isoladamente ou em combinação ao tampão de extrato fosfato de potássio 0,2 M ou à água destilada, na extração de peroxidase insolúvel de carambola, sendo que a melhor combinação foi tampão fosfato 0,2 M pH 8,0 contendo 0,2 M CaCI2, 2% PEG e 0,01 M de EDTA. O extrato total, obtido pela extração com os aditivos acima citados e 0,1% de Triton X-10O, rendeu 1,29 vezes mais POD que a soma das extrações em seqüência: 1) Enzima Livre: extraída em água destilada, contendo PEG e EDTA, ressuspendendo e extraindo o precipitado por duas vezes; 2) Enzima ionicamente ligada: ressuspendendo o último precipitado de (1) em tampão fosfato de potássio 0,2 M pH 8,0, contendo CaCb, repetindo a operação por duas vezes e, 3) Enzima solúvel com Triton X-100: ressuspensão do último precipitado de (2) no tampão de extração (2), contendo 0,1% de Triton…

Advisors/Committee Members: UNIVERSIDADE ESTADUAL DE CAMPINAS, Pastore, Glaucia Maria, 1953-, Sato, Helia Harumi, Menezes, Hilary Castle de, Maugeri, Francisco, Pereira, Jose Luiz.

Subjects/Keywords: Peroxidase

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APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6^th Edition):

Holschuh, H. J. (2000). Isolamento, purificação e caracterização bioquimica da peroxidase de carambola (Averrhoa carambola, L.). (Doctoral Dissertation). Universidade Estadual de Campinas. Retrieved from HOLSCHUH, Heinz Johann. Isolamento, purificação e caracterização bioquimica da peroxidase de carambola (Averrhoa carambola, L.). 2000. 159p. Tese (doutorado) - Universidade Estadual de Campinas, Faculdade de Engenharia de Alimentos, Campinas, SP. Disponível em: <http://www.repositorio.unicamp.br/handle/REPOSIP/256682>. Acesso em: 26 jul. 2018. ; http://repositorio.unicamp.br/jspui/handle/REPOSIP/256682

Chicago Manual of Style (16^th Edition):

Holschuh, Heinz Johann. “Isolamento, purificação e caracterização bioquimica da peroxidase de carambola (Averrhoa carambola, L.).” 2000. Doctoral Dissertation, Universidade Estadual de Campinas. Accessed April 17, 2021. HOLSCHUH, Heinz Johann. Isolamento, purificação e caracterização bioquimica da peroxidase de carambola (Averrhoa carambola, L.). 2000. 159p. Tese (doutorado) - Universidade Estadual de Campinas, Faculdade de Engenharia de Alimentos, Campinas, SP. Disponível em: <http://www.repositorio.unicamp.br/handle/REPOSIP/256682>. Acesso em: 26 jul. 2018. ; http://repositorio.unicamp.br/jspui/handle/REPOSIP/256682.

MLA Handbook (7^th Edition):

Holschuh, Heinz Johann. “Isolamento, purificação e caracterização bioquimica da peroxidase de carambola (Averrhoa carambola, L.).” 2000. Web. 17 Apr 2021.

Vancouver:

Holschuh HJ. Isolamento, purificação e caracterização bioquimica da peroxidase de carambola (Averrhoa carambola, L.). [Internet] [Doctoral dissertation]. Universidade Estadual de Campinas; 2000. [cited 2021 Apr 17]. Available from: HOLSCHUH, Heinz Johann. Isolamento, purificação e caracterização bioquimica da peroxidase de carambola (Averrhoa carambola, L.). 2000. 159p. Tese (doutorado) - Universidade Estadual de Campinas, Faculdade de Engenharia de Alimentos, Campinas, SP. Disponível em: <http://www.repositorio.unicamp.br/handle/REPOSIP/256682>. Acesso em: 26 jul. 2018. ; http://repositorio.unicamp.br/jspui/handle/REPOSIP/256682.

Council of Science Editors:

Holschuh HJ. Isolamento, purificação e caracterização bioquimica da peroxidase de carambola (Averrhoa carambola, L.). [Doctoral Dissertation]. Universidade Estadual de Campinas; 2000. Available from: HOLSCHUH, Heinz Johann. Isolamento, purificação e caracterização bioquimica da peroxidase de carambola (Averrhoa carambola, L.). 2000. 159p. Tese (doutorado) - Universidade Estadual de Campinas, Faculdade de Engenharia de Alimentos, Campinas, SP. Disponível em: <http://www.repositorio.unicamp.br/handle/REPOSIP/256682>. Acesso em: 26 jul. 2018. ; http://repositorio.unicamp.br/jspui/handle/REPOSIP/256682

University of Alberta

7. Liu, Tianzhen. Tissue-specific gene expression of two class III Arabidopsis peroxidases under aluminum stress.

Degree: MS, Department of Biological Sciences, 2010, University of Alberta

URL: https://era.library.ualberta.ca/files/6d56zx52j

► Class III peroxidases have been identified as secreted proteins involved in plant defense, auxin metabolism, cell wall modification, and regulation of reactive oxygen species. Transcriptome… (more)

Subjects/Keywords: aluminum; peroxidase; stress

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APA (6^th Edition):

Liu, T. (2010). Tissue-specific gene expression of two class III Arabidopsis peroxidases under aluminum stress. (Masters Thesis). University of Alberta. Retrieved from https://era.library.ualberta.ca/files/6d56zx52j

Chicago Manual of Style (16^th Edition):

Liu, Tianzhen. “Tissue-specific gene expression of two class III Arabidopsis peroxidases under aluminum stress.” 2010. Masters Thesis, University of Alberta. Accessed April 17, 2021. https://era.library.ualberta.ca/files/6d56zx52j.

MLA Handbook (7^th Edition):

Liu, Tianzhen. “Tissue-specific gene expression of two class III Arabidopsis peroxidases under aluminum stress.” 2010. Web. 17 Apr 2021.

Vancouver:

Liu T. Tissue-specific gene expression of two class III Arabidopsis peroxidases under aluminum stress. [Internet] [Masters thesis]. University of Alberta; 2010. [cited 2021 Apr 17]. Available from: https://era.library.ualberta.ca/files/6d56zx52j.

Council of Science Editors:

Liu T. Tissue-specific gene expression of two class III Arabidopsis peroxidases under aluminum stress. [Masters Thesis]. University of Alberta; 2010. Available from: https://era.library.ualberta.ca/files/6d56zx52j

8. Lima, Antônio Augusto Guimarães. Estudo da correlação dos níveis séricos de citocinas (IL-1β, IL-6, IL-18BP, IL-33 E TNF-α) e da atividade da mieloperoxidase com o grau de obstrução coronariana em pacientes com hipótese diagnóstica de doença isquêmica do miocárdio.

Degree: 2012, Brazil

URL: http://www.repositorio.ufc.br/handle/riufc/5545

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Atherosclerosis is a complex multifactorial disease characterized by accumulation of inflammatory cells, lipoproteins, and fibrous tissue in the walls of large and medium arteries. The innate and adaptive immunity, with the presence of leukocytes, mainly monocytes and lymphocytes, have an important role in this process. This participation can take place by signaling with cytokines and the release of the enzyme myeloperoxidase (MPO) by the cytoplasmic granules. Cardiovascular risk factors classically play an important role in prevention, however, the majority of patients with CV events have one or no risk factor. Therefore new biomarkers are needed to define diagnosis and prognosis. This study selected patients with a diagnosis of stable angina (SA) or acute coronary syndrome (ACS) undergoing coronary angiography and evaluated by the Gensini score (GS). Performed serum activity MPO, serum tumor necrosis factor alpha (TNF-α), interleukins (1β, 6, 18bp and 33) (IL-1β, IL-6, IL-18bp, and IL-33, respectively). In two years carried out a review of medical records or telephone interviews in 93 patients in this sample. Used to analyze the variables: atherosclerotic burden (carotid, coronary or lower limb atherosclerosis); the clinical picture in two years (asymptomatic or chest pain or death); clinical presentation (SA or ACS); cardiovascular events (stent, CABG, chest pain or death). The results combinations of cytokines and myeloperoxidase, with the variables presented demonstrate that IL-6 related in univariate analysis with the presence of atherosclerotic load (p <0.014), elevated serum levels of IL-18bp in patients with ACS both in univariate and multivariate analysis (p <0.001 and p <0.045 respectively), IL-1β was negatively correlated with the degree of GS in univariate and multivariate analysis (p <0.042 and <0.002 respectively); in a univariate analysis associated with the GS on patients who had chest pain or death, undergoing CABG, with CV events and ACS (p <0.001 for all). In multivariate analysis, patients with higher GS underwent CABG more often and had more chest pain or death (p <0.001 for all). The MPO activity showed no correlation or association with different variables. Patients with diabetes mellitus and in use of statin had higher GS (p <0.001 for both). In conclusion, patients with coronary stenosis were important predictors of cardiovascular events and more often underwent CABG. The IL-1β correlated…

Advisors/Committee Members: Ribeiro , Ronaldo de Albuquerque.

Subjects/Keywords: Peroxidase; Citocinas; Aterosclerose

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APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6^th Edition):

Lima, A. A. G. (2012). Estudo da correlação dos níveis séricos de citocinas (IL-1β, IL-6, IL-18BP, IL-33 E TNF-α) e da atividade da mieloperoxidase com o grau de obstrução coronariana em pacientes com hipótese diagnóstica de doença isquêmica do miocárdio. (Doctoral Dissertation). Brazil. Retrieved from http://www.repositorio.ufc.br/handle/riufc/5545

Chicago Manual of Style (16^th Edition):

Lima, Antônio Augusto Guimarães. “Estudo da correlação dos níveis séricos de citocinas (IL-1β, IL-6, IL-18BP, IL-33 E TNF-α) e da atividade da mieloperoxidase com o grau de obstrução coronariana em pacientes com hipótese diagnóstica de doença isquêmica do miocárdio.” 2012. Doctoral Dissertation, Brazil. Accessed April 17, 2021. http://www.repositorio.ufc.br/handle/riufc/5545.

MLA Handbook (7^th Edition):

Lima, Antônio Augusto Guimarães. “Estudo da correlação dos níveis séricos de citocinas (IL-1β, IL-6, IL-18BP, IL-33 E TNF-α) e da atividade da mieloperoxidase com o grau de obstrução coronariana em pacientes com hipótese diagnóstica de doença isquêmica do miocárdio.” 2012. Web. 17 Apr 2021.

Vancouver:

Lima AAG. Estudo da correlação dos níveis séricos de citocinas (IL-1β, IL-6, IL-18BP, IL-33 E TNF-α) e da atividade da mieloperoxidase com o grau de obstrução coronariana em pacientes com hipótese diagnóstica de doença isquêmica do miocárdio. [Internet] [Doctoral dissertation]. Brazil; 2012. [cited 2021 Apr 17]. Available from: http://www.repositorio.ufc.br/handle/riufc/5545.

Council of Science Editors:

Lima AAG. Estudo da correlação dos níveis séricos de citocinas (IL-1β, IL-6, IL-18BP, IL-33 E TNF-α) e da atividade da mieloperoxidase com o grau de obstrução coronariana em pacientes com hipótese diagnóstica de doença isquêmica do miocárdio. [Doctoral Dissertation]. Brazil; 2012. Available from: http://www.repositorio.ufc.br/handle/riufc/5545

9. Lazzarotto, Fernanda. Caracterização de um novo membro da superfamília de peroxidases não animais : ascorbato peroxidase-relacionada.

Degree: 2015, Brazil

URL: http://hdl.handle.net/10183/131943

►

Peroxidases atuam catalisando a redução do peróxido de hidrogênio à água a fim de minimizar o dano celular e modular, direta ou indiretamente, respostas celulares… (more)

▼

Peroxidases atuam catalisando a redução do peróxido de hidrogênio à água a fim de minimizar o dano celular e modular, direta ou indiretamente, respostas celulares dependentes da sinalização operada por esta espécie reativa de oxigênio. Análises prévias, feitas em bancos de dados de sequências genômicas, permitiram a identificação de uma nova heme peroxidase não-animal (ascorbato peroxidase-relacionada ou APx-R), a qual foi descrita pela primeira vez em 2011 em um estudo publicado pelo nosso grupo de pesquisa. O trabalho detalhado nos próximos capítulos desta tese teve como objetivo caracterizar a participação de APx-R no metabolismo antioxidante vegetal através de abordagens filogenéticas e funcionais. Os resultados apresentados nos capítulos dois e três mostram que APx-R é uma peroxidase de classe I, filogeneticamente relacionada à ascorbato peroxidase, citocromo-c peroxidase e catalase peroxidase. Em Arabidopsis thaliana, APx-R codifica uma proteína cloroplastídica que atua regulando os processos de germinação e maturação da semente. A superexpressão de APx-R in planta afetou drasticamente a viabilidade das sementes, sugerindo que os níveis de expressão deste gene devem ser rigorosamente controlados para permitir o desenvolvimento da planta. Além disso, as análises filogenéticas aqui apresentadas levaram à identificação de uma nova família de peroxidases (intitulada ascorbato peroxidase-like ou APx-L), adicionando um novo componente ao complexo sistema antioxidante vegetal.

Peroxidases act reducing hydrogen peroxide into water, minimizing cell injury and modulating cell responses through hydrogen peroxide signaling. From analysis in public genome databases, we identified a non-animal heme-peroxidase (ascorbate peroxidase-related or APx-R) present from basal to vascular plants, which was initially described in a study published by our group in 2011. The work described hereafter aimed to characterize APx-R participation in the antioxidant metabolism through phylogenetic and functional approaches. The results presented on chapters two and three showed that APx-R is a class I peroxidase, phylogenetically related to ascorbate peroxidase, cytochrome-c peroxidase and catalase peroxidase. In Arabidopsis thaliana, APx-R gene encodes a chloroplast protein which acts regulating germination and seed maturation processes. The overexpression of APx-R in planta impaired seed viability, showing that APx-R expression level must be tightly controlled in order to enable plants to develop properly. In addition, the phylogenetic analysis here presented allowed the identification of a new peroxidase family, called ascorbate peroxidase-like (APx-L), which adds a new component into plant antioxidant metabolism.

Advisors/Committee Members: Margis-Pinheiro, Márcia, Maraschin, Felipe dos Santos.

Subjects/Keywords: Peroxidase; Ascorbato peroxidases

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APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6^th Edition):

Lazzarotto, F. (2015). Caracterização de um novo membro da superfamília de peroxidases não animais : ascorbato peroxidase-relacionada. (Doctoral Dissertation). Brazil. Retrieved from http://hdl.handle.net/10183/131943

Chicago Manual of Style (16^th Edition):

Lazzarotto, Fernanda. “Caracterização de um novo membro da superfamília de peroxidases não animais : ascorbato peroxidase-relacionada.” 2015. Doctoral Dissertation, Brazil. Accessed April 17, 2021. http://hdl.handle.net/10183/131943.

MLA Handbook (7^th Edition):

Lazzarotto, Fernanda. “Caracterização de um novo membro da superfamília de peroxidases não animais : ascorbato peroxidase-relacionada.” 2015. Web. 17 Apr 2021.

Vancouver:

Lazzarotto F. Caracterização de um novo membro da superfamília de peroxidases não animais : ascorbato peroxidase-relacionada. [Internet] [Doctoral dissertation]. Brazil; 2015. [cited 2021 Apr 17]. Available from: http://hdl.handle.net/10183/131943.

Council of Science Editors:

Lazzarotto F. Caracterização de um novo membro da superfamília de peroxidases não animais : ascorbato peroxidase-relacionada. [Doctoral Dissertation]. Brazil; 2015. Available from: http://hdl.handle.net/10183/131943

Freie Universität Berlin

10. Pitsch, Nicola T. Vergleich des chloroplastidären Peroxidase-Systems und Charakterisierung der thylakoid-gebundenen APx in Physcomitrella patens.

Degree: 2013, Freie Universität Berlin

URL: https://refubium.fu-berlin.de/handle/fub188/11772

► Die Endosymbiose eines Cyanobacteriums durch eine eukaryotische Zelle führte zur Entstehung von Pflanzen und deren photosynthetischer Aktivität. Reaktive Sauerstoffspezies (engl. Reactive Oxygen Species, ROS), wie… (more)

▼ Die Endosymbiose eines Cyanobacteriums durch eine eukaryotische Zelle führte zur Entstehung von Pflanzen und deren photosynthetischer Aktivität. Reaktive Sauerstoffspezies (engl. Reactive Oxygen Species, ROS), wie Superoxidanionen, Wasserstoffperoxid und Hydroxylradikale, sind Nebenprodukte dieses Sauerstoff produzierenden Prozesses. Diese Stoffe können durch Oxidation von Lipiden, Proteinen und DNA schwere Schäden verursachen. In Chloroplasten fungieren Ascorbatperoxidasen (APxs), Peroxiredoxine (Prxs) und Glutathionperoxidasen (GPxs) als Peroxidfänger. Die vorliegende Studie fokussiert auf diese Enzymgruppen. Sie behandelt ihr Vorkommen in verschiedenen pflanzlichen Entwicklungsstufen. Die Genome der Modellsamenpflanze Arabidopsis thaliana, des Lycophyten Selaginella moellendorffii, des Laubmooses Physcomitrella patens und der Grünalge Chlamydomonas reinhardtii wurden bezüglich der für chloroplastidäre Peroxidasen kodierenden Gene analysiert. Das Arabidopsis Genom enthält ein Gen für eine stromale (sAPx) und eins für eine an Thylakoiden gebundene APx (tAPx). Zusätzlich sind zwei 2-Cys Peroxiredoxine (2CPs), ein Peroxiredoxin Q (PrxQ), ein Peroxiredoxin Typ II (PrxII) und zwei GPxs vorhanden. Diese Arbeit zeigt, dass Selaginella Chloroplasten das gleiche Set an Peroxidasen mit dem Zusatz einer weiteren PrxQ und einer GPx enthalten. Im Physcomitrella Genom jedoch, ist keine sAPx kodiert während Gene für andere chloroplastidäre Peroxidasen vervielfacht wurden. Das Vorhandensein zweier 2CPs, zweier PrxQs, dreier PrxIIs und dreier GPxs könnte einen Versuch darstellen, das Fehlen der sAPx auszugleichen. In dem Genom von Chlamydomonas konnten zwei Gene kodierend für sAPxs, drei für 2CPs, eines für PrxQ, eines für PrxII und drei für GPxs identifiziert werden. Diese Resultate zeigen, dass die Zusammensetzung des chloroplastidären antioxidativen Schutzes während der Pflanzenevolution starke Veränderungen erfuhr. Alle drei Peroxidasetypen waren in den untersuchten Pflanzenarten vertreten, was einen starken evolutionären Druck bezüglich ihres Erhalts erkennen lässt. Diese Enzyme sind essentiell, um eine ausreichende Fitness und damit das Überleben der Pflanzen über die Zeiten zu gewährleisten. EST-Daten wiesen darauf hin, dass 2CPs die am stärksten exprimierten chloroplastidären antioxidativen Enzyme in Chlamydomonas, Selaginella und Arabidopsis sind. Im Gegensatz dazu zeigte Physcomitrella eine starke Transkription der tAPx (PptAPx). Die atypische Struktur des kodierenden Gens und dessen Umgebung im Genom ließen auf einen retrotransposonalen Ursprung schließen. Eine expressionale Regulation wurde im Anschluss an die Integration von PptAPx ins Genom etabliert. Die Transkription wird an zwei unterschiedlichen Stellen initiiert und zeigte sich beeinflusst von Lichtintensität, Temperatur, niedermolekularen Antioxidantien und dem Phytohormon Abszisinsäure. Ferner wurde die Chloroplastenlokalisation von PptAPx nachgewiesen und die Funktionalität des Enzyms untersucht. Diese tAPx blieb in Physcomitrella erhalten und eine… Advisors/Committee Members: [email protected] (contact), w (gender), Margarete Baier (firstReferee), Tina Romeis (furtherReferee).

Subjects/Keywords: chloroplast; antioxidant; peroxidase; Phscomitrella; ascorbate peroxidase; peroxiredoxins; glutathione peroxidase; 500 Naturwissenschaften und Mathematik

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APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6^th Edition):

Pitsch, N. T. (2013). Vergleich des chloroplastidären Peroxidase-Systems und Charakterisierung der thylakoid-gebundenen APx in Physcomitrella patens. (Thesis). Freie Universität Berlin. Retrieved from https://refubium.fu-berlin.de/handle/fub188/11772

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Chicago Manual of Style (16^th Edition):

Pitsch, Nicola T. “Vergleich des chloroplastidären Peroxidase-Systems und Charakterisierung der thylakoid-gebundenen APx in Physcomitrella patens.” 2013. Thesis, Freie Universität Berlin. Accessed April 17, 2021. https://refubium.fu-berlin.de/handle/fub188/11772.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

MLA Handbook (7^th Edition):

Pitsch, Nicola T. “Vergleich des chloroplastidären Peroxidase-Systems und Charakterisierung der thylakoid-gebundenen APx in Physcomitrella patens.” 2013. Web. 17 Apr 2021.

Vancouver:

Pitsch NT. Vergleich des chloroplastidären Peroxidase-Systems und Charakterisierung der thylakoid-gebundenen APx in Physcomitrella patens. [Internet] [Thesis]. Freie Universität Berlin; 2013. [cited 2021 Apr 17]. Available from: https://refubium.fu-berlin.de/handle/fub188/11772.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Council of Science Editors:

Pitsch NT. Vergleich des chloroplastidären Peroxidase-Systems und Charakterisierung der thylakoid-gebundenen APx in Physcomitrella patens. [Thesis]. Freie Universität Berlin; 2013. Available from: https://refubium.fu-berlin.de/handle/fub188/11772

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

NSYSU

11. Su, Ying-Chang. Effect of INF1 protein on anionic peroxidase genes in tobacco leaves during the Hypersensitive Response.

Degree: Master, Biological Sciences, 2005, NSYSU

URL: http://etd.lib.nsysu.edu.tw/ETD-db/ETD-search/view_etd?URN=etd-0818105-104050

none Advisors/Committee Members: none (chair), none (chair), none (committee member).

Subjects/Keywords: peroxidase; INF1

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APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6^th Edition):

Su, Y. (2005). Effect of INF1 protein on anionic peroxidase genes in tobacco leaves during the Hypersensitive Response. (Thesis). NSYSU. Retrieved from http://etd.lib.nsysu.edu.tw/ETD-db/ETD-search/view_etd?URN=etd-0818105-104050

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Chicago Manual of Style (16^th Edition):

Su, Ying-Chang. “Effect of INF1 protein on anionic peroxidase genes in tobacco leaves during the Hypersensitive Response.” 2005. Thesis, NSYSU. Accessed April 17, 2021. http://etd.lib.nsysu.edu.tw/ETD-db/ETD-search/view_etd?URN=etd-0818105-104050.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

MLA Handbook (7^th Edition):

Su, Ying-Chang. “Effect of INF1 protein on anionic peroxidase genes in tobacco leaves during the Hypersensitive Response.” 2005. Web. 17 Apr 2021.

Vancouver:

Su Y. Effect of INF1 protein on anionic peroxidase genes in tobacco leaves during the Hypersensitive Response. [Internet] [Thesis]. NSYSU; 2005. [cited 2021 Apr 17]. Available from: http://etd.lib.nsysu.edu.tw/ETD-db/ETD-search/view_etd?URN=etd-0818105-104050.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Council of Science Editors:

Su Y. Effect of INF1 protein on anionic peroxidase genes in tobacco leaves during the Hypersensitive Response. [Thesis]. NSYSU; 2005. Available from: http://etd.lib.nsysu.edu.tw/ETD-db/ETD-search/view_etd?URN=etd-0818105-104050

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

12. Perkins, Arden. Model systems for structural investigations into peroxiredoxin catalysis, conformation change, and inactivation.

Degree: PhD, Biochemistry & Biophysics, 2015, Oregon State University

URL: http://hdl.handle.net/1957/55563

► Peroxiredoxin (Prx) enzymes catalyze the reduction of hydrogen peroxide, peroxynitrous acid, and organic peroxides, and are extremely efficient peroxidases, with k[subscript cat]/K[subscript M] on the… (more)

▼ Peroxiredoxin (Prx) enzymes catalyze the reduction of hydrogen peroxide, peroxynitrous acid, and organic peroxides, and are extremely efficient peroxidases, with k[subscript cat]/K[subscript M] on the order of 10⁷ - 10⁸ M⁻¹ s⁻¹. Besides their role in oxidative stress defense, evidence has accumulated that some eukaryotes, including humans, use Prxs as switches to regulate peroxide levels for the purpose of signaling events triggered by hormones and growth factors. Their significance and relevance to human health is underscored by the occurrence of cancer in some Prx knockout mice; the overexpression of Prxs in certain cancers, and knockout/knockdown studies that show Prxs in pathogens can be important, and even essential, for pathogen viability and infectivity. Further, their ubiquity in all the kingdoms of life implies Prxs provide indispensible functions. This thesis reports on work aimed at characterizing aspects of Prx function and catalysis using model systems that behave well for experimentation, specifically focusing on detangling the multifaceted roles of conserved residues, catalytic conformation change, and hyperoxidative inactivation. Five chapters of original work include two review articles and three primary research reports. One review provides a relatively broad overview of Prx structure-function (Chapter 2) and the other focuses on observations related to understanding the physiological role(s) of Prxs especially summarizing the results of knockout/knockdown studies and assessing the natural distribution of an enzyme, sulfiredoxin, that is able to reactivate hyperoxidized Prxs (Chapter 3). The latter shows that many virulent bacterial and eukaryotic pathogens lack sulfiredoxin, implying that they are unable to rescue hyperoxidatively inactivated Prxs. Of the primary research reports, two studies using the model Prx Salmonella typhimurium alkyl hydroperoxide reductase C (StAhpC) assess the impact of modifications on structure and dynamics (Chapter 4) and define the roles of highly conserved residues as they pertain to catalysis, conformation change, and oligomerization (Chapter 5). The studies with StAhpC were enabled by the discovery that a previously studied crystal form of the locally-unfolded (LU) conformation of StAhpC is also able to accommodate the fully-folded (FF) conformation. The work includes presentations of the first crystal structure of the wild type enzyme in its substrate-ready form and also the structures of eight mutants of residues that are well-conserved in the Prx1 subfamily of Prxs. The work led to an awareness of how small shifts in the relative stabilities of the FF versus LU conformations could strongly influence Prx function, and this in turn led to the proposal of a novel idea for the design of selective inhibitors of Prxs as potential drug leads: to target regions involved in the catalytic conformation change to trap them in inactive states. The third primary research report (Chapter 6) presents an analysis of three crystal structures of the PrxQ subfamily that had been… Advisors/Committee Members: Karplus, Andy (advisor), Johnson, Colin (committee member).

Subjects/Keywords: biochemistry; Peroxidase – Physiological effect

11 more images…

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APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6^th Edition):

Perkins, A. (2015). Model systems for structural investigations into peroxiredoxin catalysis, conformation change, and inactivation. (Doctoral Dissertation). Oregon State University. Retrieved from http://hdl.handle.net/1957/55563

Chicago Manual of Style (16^th Edition):

Perkins, Arden. “Model systems for structural investigations into peroxiredoxin catalysis, conformation change, and inactivation.” 2015. Doctoral Dissertation, Oregon State University. Accessed April 17, 2021. http://hdl.handle.net/1957/55563.

MLA Handbook (7^th Edition):

Perkins, Arden. “Model systems for structural investigations into peroxiredoxin catalysis, conformation change, and inactivation.” 2015. Web. 17 Apr 2021.

Vancouver:

Perkins A. Model systems for structural investigations into peroxiredoxin catalysis, conformation change, and inactivation. [Internet] [Doctoral dissertation]. Oregon State University; 2015. [cited 2021 Apr 17]. Available from: http://hdl.handle.net/1957/55563.

Council of Science Editors:

Perkins A. Model systems for structural investigations into peroxiredoxin catalysis, conformation change, and inactivation. [Doctoral Dissertation]. Oregon State University; 2015. Available from: http://hdl.handle.net/1957/55563

13. Chatchamon Daengkanit. Peroxidase from hevea brasitiensis leaves and its applications .

Degree: Faculty of Science (Biochemistry), 2005, Prince of Songkla University

URL: http://kb.psu.ac.th/psukb/handle/2553/1534

Subjects/Keywords: Peroxidase; Hevea

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APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6^th Edition):

Daengkanit, C. (2005). Peroxidase from hevea brasitiensis leaves and its applications . (Thesis). Prince of Songkla University. Retrieved from http://kb.psu.ac.th/psukb/handle/2553/1534

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Chicago Manual of Style (16^th Edition):

Daengkanit, Chatchamon. “Peroxidase from hevea brasitiensis leaves and its applications .” 2005. Thesis, Prince of Songkla University. Accessed April 17, 2021. http://kb.psu.ac.th/psukb/handle/2553/1534.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

MLA Handbook (7^th Edition):

Daengkanit, Chatchamon. “Peroxidase from hevea brasitiensis leaves and its applications .” 2005. Web. 17 Apr 2021.

Vancouver:

Daengkanit C. Peroxidase from hevea brasitiensis leaves and its applications . [Internet] [Thesis]. Prince of Songkla University; 2005. [cited 2021 Apr 17]. Available from: http://kb.psu.ac.th/psukb/handle/2553/1534.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Council of Science Editors:

Daengkanit C. Peroxidase from hevea brasitiensis leaves and its applications . [Thesis]. Prince of Songkla University; 2005. Available from: http://kb.psu.ac.th/psukb/handle/2553/1534

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

North Carolina State University

14. Cade, Christine Elizabeth. Isoniazid-Resistance Conferring Mutations in Mycobacterium tuberculosis KatG: Catalase, Peroxidase, and INH-NADH Adduct Formation Activities.

Degree: MS, Chemistry, 2009, North Carolina State University

URL: http://www.lib.ncsu.edu/resolver/1840.16/2478

► Mycobacterium tuberculosis catalase-peroxidase (KatG) is a bifunctional hemoprotein which activates isoniazid (INH), a pro-drug that is integral to frontline antituberculosis treatments. The activated species, an… (more)

Subjects/Keywords: tuberculosis; INH; KatG; Peroxidase; Catalase

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APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6^th Edition):

Cade, C. E. (2009). Isoniazid-Resistance Conferring Mutations in Mycobacterium tuberculosis KatG: Catalase, Peroxidase, and INH-NADH Adduct Formation Activities. (Thesis). North Carolina State University. Retrieved from http://www.lib.ncsu.edu/resolver/1840.16/2478

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Chicago Manual of Style (16^th Edition):

Cade, Christine Elizabeth. “Isoniazid-Resistance Conferring Mutations in Mycobacterium tuberculosis KatG: Catalase, Peroxidase, and INH-NADH Adduct Formation Activities.” 2009. Thesis, North Carolina State University. Accessed April 17, 2021. http://www.lib.ncsu.edu/resolver/1840.16/2478.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

MLA Handbook (7^th Edition):

Cade, Christine Elizabeth. “Isoniazid-Resistance Conferring Mutations in Mycobacterium tuberculosis KatG: Catalase, Peroxidase, and INH-NADH Adduct Formation Activities.” 2009. Web. 17 Apr 2021.

Vancouver:

Cade CE. Isoniazid-Resistance Conferring Mutations in Mycobacterium tuberculosis KatG: Catalase, Peroxidase, and INH-NADH Adduct Formation Activities. [Internet] [Thesis]. North Carolina State University; 2009. [cited 2021 Apr 17]. Available from: http://www.lib.ncsu.edu/resolver/1840.16/2478.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Council of Science Editors:

Cade CE. Isoniazid-Resistance Conferring Mutations in Mycobacterium tuberculosis KatG: Catalase, Peroxidase, and INH-NADH Adduct Formation Activities. [Thesis]. North Carolina State University; 2009. Available from: http://www.lib.ncsu.edu/resolver/1840.16/2478

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

15. Giovanella, Rafael Faria, 1988- ; Jesus, Paulo César de, 1967- . Estudo cinético da biodegradação dos corantes C.I. azul reativo 171 e C.I. azul reativo 160 catalisada pela peroxidase da raiz forte.

Degree: 2011, Universidade Regional de Blumenau

URL: http://www.bc.furb.br/docs/DS/2011/353889_1_1.pdf

Orientador: Paulo Cesar de Jesus.

Dissertação (mestrado) - Universidade Regional Blumenau, Centro de Ciências Exatas e Naturais, Programa de Pós-Graduação em Química.

Subjects/Keywords: Cinética química; Corantes Biodegradação; Peroxidase

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APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6^th Edition):

Giovanella, Rafael Faria, 1988- ; Jesus, Paulo César de, . 1. (2011). Estudo cinético da biodegradação dos corantes C.I. azul reativo 171 e C.I. azul reativo 160 catalisada pela peroxidase da raiz forte. (Masters Thesis). Universidade Regional de Blumenau. Retrieved from http://www.bc.furb.br/docs/DS/2011/353889_1_1.pdf

Chicago Manual of Style (16^th Edition):

Giovanella, Rafael Faria, 1988- ; Jesus, Paulo César de, 1967-. “Estudo cinético da biodegradação dos corantes C.I. azul reativo 171 e C.I. azul reativo 160 catalisada pela peroxidase da raiz forte.” 2011. Masters Thesis, Universidade Regional de Blumenau. Accessed April 17, 2021. http://www.bc.furb.br/docs/DS/2011/353889_1_1.pdf.

MLA Handbook (7^th Edition):

Giovanella, Rafael Faria, 1988- ; Jesus, Paulo César de, 1967-. “Estudo cinético da biodegradação dos corantes C.I. azul reativo 171 e C.I. azul reativo 160 catalisada pela peroxidase da raiz forte.” 2011. Web. 17 Apr 2021.

Vancouver:

Giovanella, Rafael Faria, 1988- ; Jesus, Paulo César de 1. Estudo cinético da biodegradação dos corantes C.I. azul reativo 171 e C.I. azul reativo 160 catalisada pela peroxidase da raiz forte. [Internet] [Masters thesis]. Universidade Regional de Blumenau; 2011. [cited 2021 Apr 17]. Available from: http://www.bc.furb.br/docs/DS/2011/353889_1_1.pdf.

Council of Science Editors:

Giovanella, Rafael Faria, 1988- ; Jesus, Paulo César de 1. Estudo cinético da biodegradação dos corantes C.I. azul reativo 171 e C.I. azul reativo 160 catalisada pela peroxidase da raiz forte. [Masters Thesis]. Universidade Regional de Blumenau; 2011. Available from: http://www.bc.furb.br/docs/DS/2011/353889_1_1.pdf

University of the Western Cape

16. Nkomo, Mbukeni Andrew. Comparative analysis of molecular and physiological responses of two canola genotypes to drought stress .

Degree: 2016, University of the Western Cape

URL: http://hdl.handle.net/11394/5298

► Food security has always been one of the priority concerns in Africa, and it is mostly threatened by drought stress due to climate change. Drought-induced… (more)

▼ Food security has always been one of the priority concerns in Africa, and it is mostly threatened by drought stress due to climate change. Drought-induced stress is one of the serious limiting factors of plant production, and it is known to impose oxidative stress as a consequence of excessive reactive oxygen species (ROS) accumulation that lead to lipid peroxidation, which is manifested as increased cell death. Hence, this study investigated the influence of drought stress on two contrasting canola genotypes (Agamax and Garnet), by monitoring their physiological and molecular changes. The results showed that the plant growth and biomass of both genotypes were significantly affected by drought stress as a consequence of excessive ROS accumulation (manifested as H₂O₂ and OH· content). However, under drought stress conditions, the reduction in biomass and shoot length was more pronounced in the Garnet genotype when compared to that of the Agamax genotype. This was further supported by the increase in lipid peroxidation and cell death, which were shown to be significantly higher in the Garnet genotype when compared to the Agamax genotype under drought stress. ROS scavenging ability which prevents oxidative stress and ultimately ROS-induced cellular damage. Hence, given the higher levels of antioxidant activity coupled with the reduction in ROS accumulation that was observed in the Agamax genotype, we suggest that the Agamax genotype might be slightly less susceptible to drought stress, when compared to the Garnet genotype. Furthermore, understanding the proteomic responses of these two contrasting genotypes that showed a marked difference in response to drought stress might help in unlocking complex biological networks of proteins underlying drought stress tolerance. Hence we use two-dimensional (2D) gel electrophoresis coupled with Matrix assisted laser desorption/ionisation-time of flight/time of flight tandem mass spectrometry (MALDI TOFTOF MS) analysis for this part of the study, in order to detect and analyze those differentially expressed proteins or proteins whose abundance levels were influenced as a consequence of drought stress. To gain additional insight into the leaf proteomes of the two canola genotypes, a protamine sulphate precipitation (PSP) method was used to remove RuBisCo and confirmed by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) analysis. A total of 55 well resolved protein spots were selected for mass spectrometry analysis of which 31 (56%) were positively identified using the selective criteria analysis (SCA). All positively identified proteins were then classified into functional categories including protein folding (3%), photosynthetic (29%), detoxification and protection (20%), and energy related proteins whereas 16% could not be classified into any functional category. Apart from spot 32 (Fe superoxide dismutase) and spot 34 (chloroplast beta-carbonic anhydrase), no further significant difference in protein expression/abundance was observed for all the… Advisors/Committee Members: Klein, Ashwil (advisor), Ludidi, Ndomelele (advisor), Ndimba, Bongani (advisor).

Subjects/Keywords: Ascorbate peroxidase; Canola; Drought stress

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APA (6^th Edition):

Nkomo, M. A. (2016). Comparative analysis of molecular and physiological responses of two canola genotypes to drought stress . (Thesis). University of the Western Cape. Retrieved from http://hdl.handle.net/11394/5298

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Chicago Manual of Style (16^th Edition):

Nkomo, Mbukeni Andrew. “Comparative analysis of molecular and physiological responses of two canola genotypes to drought stress .” 2016. Thesis, University of the Western Cape. Accessed April 17, 2021. http://hdl.handle.net/11394/5298.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

MLA Handbook (7^th Edition):

Nkomo, Mbukeni Andrew. “Comparative analysis of molecular and physiological responses of two canola genotypes to drought stress .” 2016. Web. 17 Apr 2021.

Vancouver:

Nkomo MA. Comparative analysis of molecular and physiological responses of two canola genotypes to drought stress . [Internet] [Thesis]. University of the Western Cape; 2016. [cited 2021 Apr 17]. Available from: http://hdl.handle.net/11394/5298.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Council of Science Editors:

Nkomo MA. Comparative analysis of molecular and physiological responses of two canola genotypes to drought stress . [Thesis]. University of the Western Cape; 2016. Available from: http://hdl.handle.net/11394/5298

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Oregon State University

17. Hall, Andrea Renee. Biophysical analyses of peroxiredoxins and a partner reductase.

Degree: PhD, Biochemistry and Biophysics, 2010, Oregon State University

URL: http://hdl.handle.net/1957/16146

► Peroxiredoxins (Prxs) are dominant peroxide-reducing enzymes with two important roles: they protect all organisms from oxidative damage induced by peroxides, and in eukaryotes, they participate… (more)

▼ Peroxiredoxins (Prxs) are dominant peroxide-reducing enzymes with two important roles: they protect all organisms from oxidative damage induced by peroxides, and in eukaryotes, they participate in hydrogen peroxide signaling pathways. This dissertation presents studies aimed at the biophysical characterization of select Prxs and a Prx reductase to elucidate their structure-function relationships. It includes two Chapters containing published (or submitted) review articles and three Chapters describing original research, two of which are published papers. A final conclusions Chapter describes the major contributions of this work and future studies. The first review presents the features of both general Prx structure and those unique to each of the six Prx subfamilies. Analysis of the universal Prx active site leads to the novel insight that the catalytic power stems from activation of both enzyme and substrate. The second review describes structural features that allow floodgate-like Prxs to participate in signaling pathways and also surveys the evidence in support of the three proposed models of Prx involvement in redox-based signaling. Two of the Chapters containing original research explore the Prx structural features associated with peroxide reduction. The first is a published analysis of the structural transition required for catalysis in the Tpx subfamily. The identified importance of the dimer interface during catalytic gymnastics and in binding substrate led to the proposal that Tpxs are obligate dimers. The second study provides structural data supporting the insights on catalytic power presented in Chapter 2. Analysis of a novel structure of human PrxV bound to DTT as well as other structures reveals how the active site stabilizes the transition state of the reaction. This Chapter also proposes diols as a novel class of competitive inhibitors. The third original research Chapter is a published characterization of a Prx reductase, the N-terminal domain of the bacterial AhpF (NTD). NMR and fluorescence measurements show that on a timescale relevant to catalysis, the oxidized form of the NTD is more heterogeneous than the reduced form. It also documents how the two thioredoxin folds that make up the NTD have evolved specialized dynamics properties related to the functional fusion of the two folds. Advisors/Committee Members: Karplus, P. Andrew (advisor), Barbar, Elisar J (committee member).

Subjects/Keywords: peroxiredoxin; Peroxidase – Structure-activity relationships

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APA (6^th Edition):

Hall, A. R. (2010). Biophysical analyses of peroxiredoxins and a partner reductase. (Doctoral Dissertation). Oregon State University. Retrieved from http://hdl.handle.net/1957/16146

Chicago Manual of Style (16^th Edition):

Hall, Andrea Renee. “Biophysical analyses of peroxiredoxins and a partner reductase.” 2010. Doctoral Dissertation, Oregon State University. Accessed April 17, 2021. http://hdl.handle.net/1957/16146.

MLA Handbook (7^th Edition):

Hall, Andrea Renee. “Biophysical analyses of peroxiredoxins and a partner reductase.” 2010. Web. 17 Apr 2021.

Vancouver:

Hall AR. Biophysical analyses of peroxiredoxins and a partner reductase. [Internet] [Doctoral dissertation]. Oregon State University; 2010. [cited 2021 Apr 17]. Available from: http://hdl.handle.net/1957/16146.

Council of Science Editors:

Hall AR. Biophysical analyses of peroxiredoxins and a partner reductase. [Doctoral Dissertation]. Oregon State University; 2010. Available from: http://hdl.handle.net/1957/16146

Oregon State University

18. Yee, Kelsey L. The role of manganese peroxidase in biomass conversion technologies.

Degree: PhD, Chemical Engineering, 2010, Oregon State University

URL: http://hdl.handle.net/1957/17700

► Currently, the technologies used to separate lignocellulosic biomass into its component parts (cellulose, hemicellulose, and lignin) and enzymatically hydrolyze the cellulose to glucose for conversion… (more)

▼ Currently, the technologies used to separate lignocellulosic biomass into its component parts (cellulose, hemicellulose, and lignin) and enzymatically hydrolyze the cellulose to glucose for conversion to ethanol could be improved economically and in terms of efficiency. A major impediment to utilizing the biomass is the presence of residual lignin. The residual lignin "poisons" the cellulase enzymes and as a result, a lower glucose yield is obtained. A higher titer of cellulases could be used to increase the yield of glucose, but cellulases are expensive. A possibility to reduce the cost of cellulase enzymes and improve the efficiency, economics, extent and/or rate of hydrolysis is to use lignin-degrading fungal heme peroxidase such as manganese peroxidases. An efficient and economical glucose assay was developed to monitor the rate and extent of enzymatic hydrolysis of cellulose. The glucose assay is based on the glucose oxidase horseradish peroxidase enzymatic method, but uses bulk enzymes making it more economical than commercial kits. The glucose assay also has a higher throughput rate and is more economical than HPLC. In order to evaluate possible synergistic effects between cellulases and manganese peroxidase (MnP), rMnP was produced in high cell density fed-batch cultivations by the genetically engineered yeast, P. pastoris. In addition, a mathematic model was developed to describe the temperature dependant growth of P. pastoris and consumption of glucose and the production and temperature dependent degradation of rMnP in the bioreactor broth. The model successfully predicted the cell growth, substrate consumption, and rMnP production for the base case and also for cultivations with varying fed-batch air flow rates (k[subscript L]a) and temperatures. The production of rMnP requires cultures amended with exogenous heme and there are several sources of heme. Through shake flask experiments and bioreactor cultivations it was determined that 0.1 g/L of heme was necessary for producing high titers of rMnP (4,500 U/L). It was also determined that not all types of heme will yield the same rMnP titer. The water soluble fraction post pretreatment of lignocellulosic biomass contains inhibitors to fermentation such as 5-hydroxymethyl furfural (HMF) and furfural. rMnP was shown to degrade HMF (1 g/L) and furfural (1 g/L) and detoxify medium containing these inhibitors. The rMnP reduced furfural and HMF, measured by absorbance at 276 and 286 nm respectively and the degree of absorbance decrease was dependent on rMnP concentration. Furfural was more readily degraded by rMnP than HMF. Growth assays using S. cerevisiae indicated rMnP treatment detoxified medium containing furfural and HMF. The optimal conditions (temperature, pH, and buffer) for enzyme activity were determined for both AccelleraseTM 1000 (commercially available combination of cellulases) and rMnP using filter paper as a substrate. Woody biomass and corn stover were pretreated and then exposed to simultaneous or… Advisors/Committee Members: Kelly, Christine J. (advisor), Lajoie, Curtis (committee member).

Subjects/Keywords: Manganese Peroxidase; Biomass conversion

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APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6^th Edition):

Yee, K. L. (2010). The role of manganese peroxidase in biomass conversion technologies. (Doctoral Dissertation). Oregon State University. Retrieved from http://hdl.handle.net/1957/17700

Chicago Manual of Style (16^th Edition):

Yee, Kelsey L. “The role of manganese peroxidase in biomass conversion technologies.” 2010. Doctoral Dissertation, Oregon State University. Accessed April 17, 2021. http://hdl.handle.net/1957/17700.

MLA Handbook (7^th Edition):

Yee, Kelsey L. “The role of manganese peroxidase in biomass conversion technologies.” 2010. Web. 17 Apr 2021.

Vancouver:

Yee KL. The role of manganese peroxidase in biomass conversion technologies. [Internet] [Doctoral dissertation]. Oregon State University; 2010. [cited 2021 Apr 17]. Available from: http://hdl.handle.net/1957/17700.

Council of Science Editors:

Yee KL. The role of manganese peroxidase in biomass conversion technologies. [Doctoral Dissertation]. Oregon State University; 2010. Available from: http://hdl.handle.net/1957/17700

Michigan State University

19. Al-Jasin, Hamid Abdullah. Effect of irradiation on peroxidase.

Degree: PhD, Department of Food Science, 1966, Michigan State University

URL: http://etd.lib.msu.edu/islandora/object/etd:34156

Subjects/Keywords: Irradiation; Peroxidase

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APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6^th Edition):

Al-Jasin, H. A. (1966). Effect of irradiation on peroxidase. (Doctoral Dissertation). Michigan State University. Retrieved from http://etd.lib.msu.edu/islandora/object/etd:34156

Chicago Manual of Style (16^th Edition):

Al-Jasin, Hamid Abdullah. “Effect of irradiation on peroxidase.” 1966. Doctoral Dissertation, Michigan State University. Accessed April 17, 2021. http://etd.lib.msu.edu/islandora/object/etd:34156.

MLA Handbook (7^th Edition):

Al-Jasin, Hamid Abdullah. “Effect of irradiation on peroxidase.” 1966. Web. 17 Apr 2021.

Vancouver:

Al-Jasin HA. Effect of irradiation on peroxidase. [Internet] [Doctoral dissertation]. Michigan State University; 1966. [cited 2021 Apr 17]. Available from: http://etd.lib.msu.edu/islandora/object/etd:34156.

Council of Science Editors:

Al-Jasin HA. Effect of irradiation on peroxidase. [Doctoral Dissertation]. Michigan State University; 1966. Available from: http://etd.lib.msu.edu/islandora/object/etd:34156

Michigan State University

20. Michel, Frederick Carl. The peroxidases of phanerochaete chrysosporium : culture modelling and application.

Degree: PhD, Department of Chemical Engineering, 1991, Michigan State University

URL: http://etd.lib.msu.edu/islandora/object/etd:23326

Subjects/Keywords: Peroxidase; Phanerochaete

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APA (6^th Edition):

Michel, F. C. (1991). The peroxidases of phanerochaete chrysosporium : culture modelling and application. (Doctoral Dissertation). Michigan State University. Retrieved from http://etd.lib.msu.edu/islandora/object/etd:23326

Chicago Manual of Style (16^th Edition):

Michel, Frederick Carl. “The peroxidases of phanerochaete chrysosporium : culture modelling and application.” 1991. Doctoral Dissertation, Michigan State University. Accessed April 17, 2021. http://etd.lib.msu.edu/islandora/object/etd:23326.

MLA Handbook (7^th Edition):

Michel, Frederick Carl. “The peroxidases of phanerochaete chrysosporium : culture modelling and application.” 1991. Web. 17 Apr 2021.

Vancouver:

Michel FC. The peroxidases of phanerochaete chrysosporium : culture modelling and application. [Internet] [Doctoral dissertation]. Michigan State University; 1991. [cited 2021 Apr 17]. Available from: http://etd.lib.msu.edu/islandora/object/etd:23326.

Council of Science Editors:

Michel FC. The peroxidases of phanerochaete chrysosporium : culture modelling and application. [Doctoral Dissertation]. Michigan State University; 1991. Available from: http://etd.lib.msu.edu/islandora/object/etd:23326

Massey University

21. Wilson, James Martin. The oxidation of chalcone catalysed by peroxidase.

Degree: PhD, Plant Science, 1971, Massey University

URL: http://hdl.handle.net/10179/3795

► This thesis deals with studies which have as their origin the intention to investigate select aspects of the enzymology of flavonoid biosynthesis and which lead… (more)

Subjects/Keywords: Chalones; Peroxidase

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APA (6^th Edition):

Wilson, J. M. (1971). The oxidation of chalcone catalysed by peroxidase. (Doctoral Dissertation). Massey University. Retrieved from http://hdl.handle.net/10179/3795

Chicago Manual of Style (16^th Edition):

Wilson, James Martin. “The oxidation of chalcone catalysed by peroxidase.” 1971. Doctoral Dissertation, Massey University. Accessed April 17, 2021. http://hdl.handle.net/10179/3795.

MLA Handbook (7^th Edition):

Wilson, James Martin. “The oxidation of chalcone catalysed by peroxidase.” 1971. Web. 17 Apr 2021.

Vancouver:

Wilson JM. The oxidation of chalcone catalysed by peroxidase. [Internet] [Doctoral dissertation]. Massey University; 1971. [cited 2021 Apr 17]. Available from: http://hdl.handle.net/10179/3795.

Council of Science Editors:

Wilson JM. The oxidation of chalcone catalysed by peroxidase. [Doctoral Dissertation]. Massey University; 1971. Available from: http://hdl.handle.net/10179/3795

22. Carvalho, Fabrício Eulálio Leite. A superexpressão de proteínas relacionadas com atividades fotoquímica e fotorespiratória induzida por silenciamento das APX citosólicas contribui para uma fotoinibição similar a de arroz não-transformado submetido à alta luz.

Degree: 2013, Brazil

URL: http://www.repositorio.ufc.br/handle/riufc/10816

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CARVALHO, F. E. L. A superexpressão de proteínas relacionadas com atividades fotoquímica e fotorespiratória induzida por silenciamento das APX citosólicas contribui para uma fotoinibição similar… (more)

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CARVALHO, F. E. L. A superexpressão de proteínas relacionadas com atividades fotoquímica e fotorespiratória induzida por silenciamento das APX citosólicas contribui para uma fotoinibição similar a de arroz não-transformado submetido à alta luz. 2013. 118 f. Dissertação (Mestrado em Bioquímica) - Centro de Ciências, Universidade Federal do Ceará, Fortaleza, 2013.

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In tropical regions, where there is a high incidence of light, electrons can accumulate in the transport chain (PET) producing large quantities of H2O2 and other ROS, which might generate photodamage and photoinhibition. To survive to these challenges, plants have developed several mechanisms to mitigate the excess energy in photosystems, besides having an efficient machinery for removal of excess H2O2, which includes cytosolic APX (cAPX). However, double-silenced rice plants for cAPX (OsAPX1/2) do not show large differences in morpho-phenotype when compared to non-transformed (NT), although OsAPX1/2 presents induction of expression on several proteins related to photosynthesis. The physiological implications of this induction, as well as its consequences for OsAPX1/2 resistance against stresses of high light (HL), are still poorly known. Aiming to clarify the role of cAPx in photosynthesis, OsAPX1/2 plants were produced, subjected to 24 hours of HL (2,000 μmol m-2s-1) and studied for the expression and activity of proteins related to photosynthesis, photorespiration and redox homeostasis. The amount of several PET proteins (Lhcb1, PsbO, PsbP, PsbQ, PSAC, PC, FNR and FDX) and Chl and Pheo were increased in OsAPX1/2 in normal growth conditions, however without causing changes in the in vivo photochemistry activity parameters (Fv/Fm and ΔFm/Fm'). In contrast, expression of proteins associated with Calvin-Benson cycle (Rls, ativase RBC) and rubisco carboxylation activity (in vivo and in vitro) were not altered in mutants under normal growth conditions. In HL, the expression of proteins related to photosynthesis was strongly repressed in all genotypes, as well as gas exchange parameters and Fv/Fm, the latter being strong indication of photoinhibition. Moreover, proteins related to photorespiration showed increased expression/activity in response to HL in NT and maintenance of already high levels in OsAPX1/2. In OsAPX1/2 the expression and activity of chloroplastic Cu/Zn-SOD showed a similar response exhibited by photorespiration-related proteins, although the activity…

Advisors/Committee Members: Silveira, Joaquim Albenísio Gomes da.

Subjects/Keywords: Bioquímica; Fotossíntese; Oryza sativa; Peroxidase

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APA (6^th Edition):

Carvalho, F. E. L. (2013). A superexpressão de proteínas relacionadas com atividades fotoquímica e fotorespiratória induzida por silenciamento das APX citosólicas contribui para uma fotoinibição similar a de arroz não-transformado submetido à alta luz. (Masters Thesis). Brazil. Retrieved from http://www.repositorio.ufc.br/handle/riufc/10816

Chicago Manual of Style (16^th Edition):

Carvalho, Fabrício Eulálio Leite. “A superexpressão de proteínas relacionadas com atividades fotoquímica e fotorespiratória induzida por silenciamento das APX citosólicas contribui para uma fotoinibição similar a de arroz não-transformado submetido à alta luz.” 2013. Masters Thesis, Brazil. Accessed April 17, 2021. http://www.repositorio.ufc.br/handle/riufc/10816.

MLA Handbook (7^th Edition):

Carvalho, Fabrício Eulálio Leite. “A superexpressão de proteínas relacionadas com atividades fotoquímica e fotorespiratória induzida por silenciamento das APX citosólicas contribui para uma fotoinibição similar a de arroz não-transformado submetido à alta luz.” 2013. Web. 17 Apr 2021.

Vancouver:

Carvalho FEL. A superexpressão de proteínas relacionadas com atividades fotoquímica e fotorespiratória induzida por silenciamento das APX citosólicas contribui para uma fotoinibição similar a de arroz não-transformado submetido à alta luz. [Internet] [Masters thesis]. Brazil; 2013. [cited 2021 Apr 17]. Available from: http://www.repositorio.ufc.br/handle/riufc/10816.

Council of Science Editors:

Carvalho FEL. A superexpressão de proteínas relacionadas com atividades fotoquímica e fotorespiratória induzida por silenciamento das APX citosólicas contribui para uma fotoinibição similar a de arroz não-transformado submetido à alta luz. [Masters Thesis]. Brazil; 2013. Available from: http://www.repositorio.ufc.br/handle/riufc/10816

23. Oliveira, Henrique Pinho. Purificação, caracterização e atividade antifúngica da Mm-POX, uma peroxidase do látex de Marsdenia megalantha (GOYDER; MORILLO, 1994).

Degree: 2013, Brazil

URL: http://www.repositorio.ufc.br/handle/riufc/14936

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The peroxidases are present in all living organisms and constitute a group of multifunctional enzymes with several biotechnological applications. In this group, the class III plant peroxidases (POX) (EC 1.11.1.7) are enzymes well characterized, with involvement in lignification, suberization, auxin catabolism, wound healing and plant defense. These enzymes have been detected in different parts of the plant, including the latex. The aim of this work was the purification, characterization and antifungal activity evaluation of a peroxidase from Marsdenia megalantha latex, an endemic species of the Caatinga. The latex was collected from plant grown in Quixadá, Ceará, Brazil, diluted (1:2) in 0.05 M Tris-HCl containing 0.15 M NaCl, pH 8.0, and subjected to centrifugation and dialysis against water. The supernatant was applied to a DEAE-Cellulose matrix previously equilibrated with 0.05 M sodium acetate buffer, pH 5.2 and two protein fractions were obtained. Elution of the non retained proteins (FnRd) was achivied by the equilibrium buffer, whereas the bound proteins (FRd) were eluted with 0.2 M NaCl in the same buffer. FnRd was subjected to a chromatography on Superose 12 HR 10/30 column, yielding two protein fractions (S1 and S2). S1 was shown to be a pure protein with peroxidasic activity, apparent molecular mass of 60 kDa, pI 5.2 and identity with other POXs, being named of M. megalantha peroxidase (Mm-POX). Mm-POX follows the Michaelis-Menten kinetics, with high affinity for guaiacol and H2O2, elevated thermal stability (60 °C, 1 hour) and optimum pH around 6.0. The catalytic activity of Mm-POX was reduced in the presence of classic peroxidases inhibitors, including azide, DTT, EDTA and Na2S2O5 and also in high concentrations of Na+, Mn2+ and salicylic acid. On the other hand, Ca2+ and Mg2+, even at low concentrations, were able to enhance the enzymatic activity of Mm-POX. In addition, Mm-POX was able to inhibit the Fusarium oxysporum and F. solani conidia germination. This action is probably due to changes in the cell membrane as well as induction of oxidative stress. The results reveal that Mm-POX is a class III peroxidase, being the first enzyme isolated from M. megalantha species, with potential use in the control of plant disease caused by fungi, adding biotechnological value to this enzyme.

As peroxidases estão presentes em todos os organismos vivos e constituem um grupo de enzimas…

Advisors/Committee Members: Vasconcelos, Ilka Maria.

Subjects/Keywords: Peroxidase; Enzimas; Atividade antifúngica

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APA (6^th Edition):

Oliveira, H. P. (2013). Purificação, caracterização e atividade antifúngica da Mm-POX, uma peroxidase do látex de Marsdenia megalantha (GOYDER; MORILLO, 1994). (Doctoral Dissertation). Brazil. Retrieved from http://www.repositorio.ufc.br/handle/riufc/14936

Chicago Manual of Style (16^th Edition):

Oliveira, Henrique Pinho. “Purificação, caracterização e atividade antifúngica da Mm-POX, uma peroxidase do látex de Marsdenia megalantha (GOYDER; MORILLO, 1994).” 2013. Doctoral Dissertation, Brazil. Accessed April 17, 2021. http://www.repositorio.ufc.br/handle/riufc/14936.

MLA Handbook (7^th Edition):

Oliveira, Henrique Pinho. “Purificação, caracterização e atividade antifúngica da Mm-POX, uma peroxidase do látex de Marsdenia megalantha (GOYDER; MORILLO, 1994).” 2013. Web. 17 Apr 2021.

Vancouver:

Oliveira HP. Purificação, caracterização e atividade antifúngica da Mm-POX, uma peroxidase do látex de Marsdenia megalantha (GOYDER; MORILLO, 1994). [Internet] [Doctoral dissertation]. Brazil; 2013. [cited 2021 Apr 17]. Available from: http://www.repositorio.ufc.br/handle/riufc/14936.

Council of Science Editors:

Oliveira HP. Purificação, caracterização e atividade antifúngica da Mm-POX, uma peroxidase do látex de Marsdenia megalantha (GOYDER; MORILLO, 1994). [Doctoral Dissertation]. Brazil; 2013. Available from: http://www.repositorio.ufc.br/handle/riufc/14936

24. Almeida, Marina Gabrielle Guimarães de. Purificação e caracterização de uma peroxidase de raízes de Moringa oleifera L e seu potencial na degradação de corantes têxteis.

Degree: 2017, Brazil

URL: http://www.repositorio.ufc.br/handle/riufc/30689

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Peroxidases are oxidoredutases that catalyze a variety of reactions such as reduction of hydrogen peroxide (H2O2) and oxidation of a variety of organic and inorganic compounds. These enzymes are widely distributed in nature, being produced by a variety of sources including plants, animals, and microorganisms. Class III plant peroxidases (EC 1.11.1.7) are enzymes well characterized and related to physiological events such as lignification, suberization, auxin catabolism, wound healing and plant defense. A peroxidase from roots of Moringa oleifera (named MoPOX) was purified, characterized, and its ability to degrade textile dyes was evaluated. MoPOX was purified by DEAE-Sephacel and Superdex 75, presented an apparent molecular mass of 45.6 kDa and a pI of 9.4. The optimum pH and temperature for MoPOX activity are 5.2 and 70 °C, respectively. MoPOX maintained at least 80% of its catalytic activity after incubation at 70 C for 60 min, showing to be high thermostable. MoPOX catalytic constants showed its high affinity for guaiacol and hydrogen peroxide substrates. In addition, it can oxidize other substrates such as o-dianidisidine, eugenol and ABTS. The catalytic activity MoPOX was decreased in the presence of dithiotreitol. In contrast, Na+ and Ca2+ slightly enhanced the MoPOX enzymatic activity. Purified MoPOX (0.15, 0.03 or 0.015 mg/mL) was able to degrade different dyes (10, 25, 50 or 100 mg/L), being Remazol® Blue RGB, Remazol® Navy RGB and Telon® Turquoise M-5G 85% the most susceptible dyes. For these compounds, the decolorization rates varied from 15 to 90%, depending on the concentration dye, concentration of enzyme, and time of exposure. MoPOX is the first peroxidase purified from roots of M. oleifera. Its high termostability, plus the ability to degrade different types of textile dyes makes this enzyme a potential molecule for application in strategies for biodegradation of hazardous compounds.

As peroxidases são oxidoredutases que catalisam uma variedade de reações tais como a redução do peróxido de hidrogênio (H2O2) e a oxidação de uma variedade de compostos orgânicos e inorgânicos. Estas enzimas são amplamente distribuídas na natureza, sendo produzidas por uma variedade de fontes, incluindo plantas, animais e microrganismos. As peroxidases de plantas da classe III (EC 1.11.1.7) são enzimas bem caracterizadas e relacionadas com papeis fisiológicos tais como lignificação, suberização,…

Advisors/Committee Members: Souza, Daniele de Oliveira Bezerra de.

Subjects/Keywords: Peroxidase; Moringa oleifera; Corantes têxteis

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APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6^th Edition):

Almeida, M. G. G. d. (2017). Purificação e caracterização de uma peroxidase de raízes de Moringa oleifera L e seu potencial na degradação de corantes têxteis. (Masters Thesis). Brazil. Retrieved from http://www.repositorio.ufc.br/handle/riufc/30689

Chicago Manual of Style (16^th Edition):

Almeida, Marina Gabrielle Guimarães de. “Purificação e caracterização de uma peroxidase de raízes de Moringa oleifera L e seu potencial na degradação de corantes têxteis.” 2017. Masters Thesis, Brazil. Accessed April 17, 2021. http://www.repositorio.ufc.br/handle/riufc/30689.

MLA Handbook (7^th Edition):

Almeida, Marina Gabrielle Guimarães de. “Purificação e caracterização de uma peroxidase de raízes de Moringa oleifera L e seu potencial na degradação de corantes têxteis.” 2017. Web. 17 Apr 2021.

Vancouver:

Almeida MGGd. Purificação e caracterização de uma peroxidase de raízes de Moringa oleifera L e seu potencial na degradação de corantes têxteis. [Internet] [Masters thesis]. Brazil; 2017. [cited 2021 Apr 17]. Available from: http://www.repositorio.ufc.br/handle/riufc/30689.

Council of Science Editors:

Almeida MGGd. Purificação e caracterização de uma peroxidase de raízes de Moringa oleifera L e seu potencial na degradação de corantes têxteis. [Masters Thesis]. Brazil; 2017. Available from: http://www.repositorio.ufc.br/handle/riufc/30689

Universidade Estadual de Campinas

25. Santos, Elen Resende. Caracterização bioquimica da peroxidase e da polifenoloxidase de açai (Euterpe oleracea).

Degree: Faculdade de Engenharia de Alimentos, 2001, Universidade Estadual de Campinas

URL: SANTOS, Elen Resende. Caracterização bioquimica da peroxidase e da polifenoloxidase de açai (Euterpe oleracea). 2001. 104p. Dissertação (mestrado) - Universidade Estadual de Campinas, Faculdade de Engenharia de Alimentos, Campinas, SP. Disponível em: <http://www.repositorio.unicamp.br/handle/REPOSIP/254326>. Acesso em: 31 jul. 2018. ; http://repositorio.unicamp.br/jspui/handle/REPOSIP/254326

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Orientador : Helia Harumi Sato

Dissertação (mestrado) - Universidade Estadual de Campinas, Faculdade de Engenharia de Alimentos

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Subjects/Keywords: Peroxidase; Açai

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APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6^th Edition):

Santos, E. R. (2001). Caracterização bioquimica da peroxidase e da polifenoloxidase de açai (Euterpe oleracea). (Masters Thesis). Universidade Estadual de Campinas. Retrieved from SANTOS, Elen Resende. Caracterização bioquimica da peroxidase e da polifenoloxidase de açai (Euterpe oleracea). 2001. 104p. Dissertação (mestrado) - Universidade Estadual de Campinas, Faculdade de Engenharia de Alimentos, Campinas, SP. Disponível em: <http://www.repositorio.unicamp.br/handle/REPOSIP/254326>. Acesso em: 31 jul. 2018. ; http://repositorio.unicamp.br/jspui/handle/REPOSIP/254326

Chicago Manual of Style (16^th Edition):

Santos, Elen Resende. “Caracterização bioquimica da peroxidase e da polifenoloxidase de açai (Euterpe oleracea).” 2001. Masters Thesis, Universidade Estadual de Campinas. Accessed April 17, 2021. SANTOS, Elen Resende. Caracterização bioquimica da peroxidase e da polifenoloxidase de açai (Euterpe oleracea). 2001. 104p. Dissertação (mestrado) - Universidade Estadual de Campinas, Faculdade de Engenharia de Alimentos, Campinas, SP. Disponível em: <http://www.repositorio.unicamp.br/handle/REPOSIP/254326>. Acesso em: 31 jul. 2018. ; http://repositorio.unicamp.br/jspui/handle/REPOSIP/254326.

MLA Handbook (7^th Edition):

Santos, Elen Resende. “Caracterização bioquimica da peroxidase e da polifenoloxidase de açai (Euterpe oleracea).” 2001. Web. 17 Apr 2021.

Vancouver:

Santos ER. Caracterização bioquimica da peroxidase e da polifenoloxidase de açai (Euterpe oleracea). [Internet] [Masters thesis]. Universidade Estadual de Campinas; 2001. [cited 2021 Apr 17]. Available from: SANTOS, Elen Resende. Caracterização bioquimica da peroxidase e da polifenoloxidase de açai (Euterpe oleracea). 2001. 104p. Dissertação (mestrado) - Universidade Estadual de Campinas, Faculdade de Engenharia de Alimentos, Campinas, SP. Disponível em: <http://www.repositorio.unicamp.br/handle/REPOSIP/254326>. Acesso em: 31 jul. 2018. ; http://repositorio.unicamp.br/jspui/handle/REPOSIP/254326.

Council of Science Editors:

Santos ER. Caracterização bioquimica da peroxidase e da polifenoloxidase de açai (Euterpe oleracea). [Masters Thesis]. Universidade Estadual de Campinas; 2001. Available from: SANTOS, Elen Resende. Caracterização bioquimica da peroxidase e da polifenoloxidase de açai (Euterpe oleracea). 2001. 104p. Dissertação (mestrado) - Universidade Estadual de Campinas, Faculdade de Engenharia de Alimentos, Campinas, SP. Disponível em: <http://www.repositorio.unicamp.br/handle/REPOSIP/254326>. Acesso em: 31 jul. 2018. ; http://repositorio.unicamp.br/jspui/handle/REPOSIP/254326

26. Itako, Adriana Terumi [UNESP]. Avaliação de produtos químicos no controle e na indução de mecanismos bioquímicos de resistência à mancha bacteriana (Xanthomonas perforans) do tomateiro.

Degree: 2012, Universidade Estadual Paulista (UNESP)

URL: http://hdl.handle.net/11449/105474

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O presente trabalho teve por objetivo avaliar em condições de casa-de-vegetação e de campo a ação de alguns fungicidas e antibiótico no controle da mancha bacteriana (Xanthomonas perforans) do tomateiro e na ativação de enzimas relacionadas à indução de resistência. A sensibilidade in vitro foi avaliada utilizando os produtos acibenzolar-S-metil; piraclostrobina e piraclostrobina + methiran, oxicloreto de cobre, oxicloreto de cobre + mancozeb, fluazinam e oxitetraciclina nas concentrações de 0; 5; 10; 50; 100; 500; 1000 e 5000 μg.mL-1. Acibenzolar- S-metil e piraclostrobina não inibiram o crescimento de X. perforans em todas as concentrações avaliadas e para os demais produtos, o crescimento bacteriano variou em função da concentração ensaiada. Para avaliação da severidade e atividade enzimática em casa-devegetação, foram utilizadas as cultivares de tomateiro Santa Clara e Gisele e o híbrido AP 529 inoculadas com X. perforans. Os tratamentos consistiram da pulverização com acibenzolar-Smetil (2,5 g i.a./100 L), fluazinam (25 g i.a./100 L), piraclostrobina (8 g i.a./100 L), piraclostrobina + methiran (20 g + 220 g i.a./100L), oxicloreto de cobre (150 g i.a./100 L), oxicloreto de cobre + mancozeb (88 g + 60 g i.a./100 L) e oxitetraciclina (40 g i.a./100 L), além de uma testemunha inoculada e uma testemunha não inoculada. Com os dados de severidade foi calculada a área abaixo da curva de progresso da doença (AACPD). Todos os tratamentos apresentaram redução da AACPD em relação à testemunha. Os fungicidas acibenzolar-S-metil, piraclostrobina e piraclostrobina + methiran tiveram a maior redução da severidade da mancha bacteriana em tomateiro em condições de casa-de-vegetação. Os produtos à base de...

This study aimed to evaluate in greenhouse and in field the action of fungicides and antibiotics against tomato’s bacterial spot (Xanthomonas perforans) and the activation of enzymes related to the resistance. The sensitivity was evaluated in vitro using the products acibenzolar-Smethyl, pyraclostrobin, pyraclostrobin + methiran, copper oxychloride, copper oxychloride + mancozeb, oxytetracycline at concentrations of 0, 5, 10, 50, 100, 500, 1000 and 5000 μg.mL- 1. Acibenzolar-S-methyl and pyraclostrobin did not inhibit the growth of X. perforans in all concentrations tested and for other products, the bacterial growth varied depending on the concentration tested. To assess the severity and enzyme activity in greenhouse, we used the tomato cultivars Santa Clara, Gisele and AP529 inoculated with X. perforans. The treatments consisted of pulverization with: acibenzolar-S-methyl (2.5 g a.i./100 L), fluazinam (25 g a.i./100 L), pyraclostrobin (8 g a.i./100 L) methiran + pyraclostrobin (20 g + 220 g i.a./100 L), copper oxychloride (150 g ai/100 L), copper oxychloride +…

Advisors/Committee Members: Universidade Estadual Paulista (UNESP), Maringoni, Antonio Carlos [UNESP], Estrada, Kátia Regina F. Schawan [UNESP].

Subjects/Keywords: Peroxidase; Tomate; Xanthomonas; Tomatoes

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APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6^th Edition):

Itako, A. T. [. (2012). Avaliação de produtos químicos no controle e na indução de mecanismos bioquímicos de resistência à mancha bacteriana (Xanthomonas perforans) do tomateiro. (Doctoral Dissertation). Universidade Estadual Paulista (UNESP). Retrieved from http://hdl.handle.net/11449/105474

Chicago Manual of Style (16^th Edition):

Itako, Adriana Terumi [UNESP]. “Avaliação de produtos químicos no controle e na indução de mecanismos bioquímicos de resistência à mancha bacteriana (Xanthomonas perforans) do tomateiro.” 2012. Doctoral Dissertation, Universidade Estadual Paulista (UNESP). Accessed April 17, 2021. http://hdl.handle.net/11449/105474.

MLA Handbook (7^th Edition):

Itako, Adriana Terumi [UNESP]. “Avaliação de produtos químicos no controle e na indução de mecanismos bioquímicos de resistência à mancha bacteriana (Xanthomonas perforans) do tomateiro.” 2012. Web. 17 Apr 2021.

Vancouver:

Itako AT[. Avaliação de produtos químicos no controle e na indução de mecanismos bioquímicos de resistência à mancha bacteriana (Xanthomonas perforans) do tomateiro. [Internet] [Doctoral dissertation]. Universidade Estadual Paulista (UNESP); 2012. [cited 2021 Apr 17]. Available from: http://hdl.handle.net/11449/105474.

Council of Science Editors:

Itako AT[. Avaliação de produtos químicos no controle e na indução de mecanismos bioquímicos de resistência à mancha bacteriana (Xanthomonas perforans) do tomateiro. [Doctoral Dissertation]. Universidade Estadual Paulista (UNESP); 2012. Available from: http://hdl.handle.net/11449/105474

27. Passaia, Gisele. Análise funcional dos genes de glutationa peroxidase em arroz (Oriza sativa) e Arabidopsis (Arabidopsis thaliana).

Degree: 2013, Brazil

URL: http://hdl.handle.net/10183/143442

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As espécies reativas de oxigênio (ERO) afetam significativamente a homeostase redox celular. No entanto, o peróxido de hidrogênio (H2O2), uma das ERO mais estudadas, é… (more)

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As espécies reativas de oxigênio (ERO) afetam significativamente a homeostase redox celular. No entanto, o peróxido de hidrogênio (H2O2), uma das ERO mais estudadas, é considerado regulador chave em uma série de processos fisiológicos, dependendo de sua concentração na célula: em baixas concentrações atua como molécula sinalizadora envolvida na aclimatação da planta a estresses, desencadeando tolerância a estresses bióticos e abióticos; por outro lado, em altas concentrações o H2O2 pode levar à morte celular. Gradientes de ERO e fitohormônios têm influência nas respostas de crescimento local e consecutivamente afetam o estado redox celular. Diversos fitohormônios afetam a sinalização redox celular controlando processos de crescimento e defesa. Os níveis de H2O2 intracelulares são controlados pela ação de diversas enzimas da classe das peroxidases e catalases. Dentre as peroxidases, a família de proteínas GPX pode ser encontrada em praticamente todos os reinos e vem sendo cada vez mais estudada em plantas. Em arroz, essa família é composta de cinco genes, enquanto em Arabidopsis foram identificados oito genes. Este trabalho teve como objetivo caracterizar funcionalmente as GPX mitocondriais e cloroplastídica de arroz e sete dos oito genes de Arabidopsis thaliana. Mutantes knockout de Arabidopsis para os genes AtGPX1, AtGPX2, AtGPX3, AtGPX4, AtGPX6, AtGPX7 e AtGPX8 foram obtidos.Nesta espécie, pelo menos AtGPX2, AtGPX3 e AtGPX6 são necessárias para a correta formação da arquitetura da raiz dependente dos hormônios ABA, auxina e SL. O sileciamento por RNAi em arroz para os genes OsGPX1, OsGPX3 e OsGPX4 gerou plantas com crescimento deficiente de raiz, parte área e formação de panículas. A redução em 80% da expressão gênica da isoforma cloroplastídica (OsGPX4) foi letal para o desenvolvimento de plântulas regeneradas a partir de calos de arroz, enquanto que a redução da expressão de 40% e 95% de OsGPX1 (GPX1s) e OsGPX3 (GPX3s), respectivamente, não impediu a regeneração de plantas. No entanto, plantas GPX1s apresentaram menor tamanho, menor número de panículas e menor produção de sementes em comparação com as plantas NT (não transformadas). Adicionalmente, plantas GPX3s apresentaram redução do comprimento tanto da parte aérea quanto das raízes, além de acúmulo de H2O2 cerca de vinte vezes maior do que a planta NT. Neste trabalho, foi demonstrada a participação das enzimas GPX durante o desenvolvimento vegetativo e reprodutivo de plantas de arroz e o estabelecimento da arquitetura da raiz dependente de hormônios em Arabidopsis. O conjunto de dados obtidos contribuempara o entendimento do papel dessas enzimas na homeostase redox, como também na interação com fitohormônios nos processos de desenvolvimento e defesa vegetais.

Reactive oxygen species (ROS) affect significantly cellular redox homeostasis. Hydrogen peroxide (H2O2), one of the most studied ROS, is considered a key regulator in a number of physiological processes dependent of its concentration in the cell: at low concentrations acts as a signaling molecule…

Advisors/Committee Members: Margis-Pinheiro, Márcia.

Subjects/Keywords: Oryza sativa; Arroz; Glutationa peroxidase

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APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6^th Edition):

Passaia, G. (2013). Análise funcional dos genes de glutationa peroxidase em arroz (Oriza sativa) e Arabidopsis (Arabidopsis thaliana). (Doctoral Dissertation). Brazil. Retrieved from http://hdl.handle.net/10183/143442

Chicago Manual of Style (16^th Edition):

Passaia, Gisele. “Análise funcional dos genes de glutationa peroxidase em arroz (Oriza sativa) e Arabidopsis (Arabidopsis thaliana).” 2013. Doctoral Dissertation, Brazil. Accessed April 17, 2021. http://hdl.handle.net/10183/143442.

MLA Handbook (7^th Edition):

Passaia, Gisele. “Análise funcional dos genes de glutationa peroxidase em arroz (Oriza sativa) e Arabidopsis (Arabidopsis thaliana).” 2013. Web. 17 Apr 2021.

Vancouver:

Passaia G. Análise funcional dos genes de glutationa peroxidase em arroz (Oriza sativa) e Arabidopsis (Arabidopsis thaliana). [Internet] [Doctoral dissertation]. Brazil; 2013. [cited 2021 Apr 17]. Available from: http://hdl.handle.net/10183/143442.

Council of Science Editors:

Passaia G. Análise funcional dos genes de glutationa peroxidase em arroz (Oriza sativa) e Arabidopsis (Arabidopsis thaliana). [Doctoral Dissertation]. Brazil; 2013. Available from: http://hdl.handle.net/10183/143442

Universidade Federal de Santa Maria

28. Jessie Haigert Sudati. TOXICOLOGIA E FARMACOLOGIA IN VITRO DE NOVOS COMPOSTOS ORGÂNICOS DE SELÊNIO E TELÚRIO COM ATIVIDADE TIPO TIOL PEROXIDASE.

Degree: 2009, Universidade Federal de Santa Maria

URL: http://coralx.ufsm.br/tede/tde_busca/arquivo.php?codArquivo=2588

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Glutathione peroxidase (GPx; EC 1.11.1.9) is a well-known selenoenzyme that catalyzes the reduction of hydrogen peroxide and some organic hydroperoxides by glutathione (GSH) and protects… (more)

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Glutathione peroxidase (GPx; EC 1.11.1.9) is a well-known selenoenzyme that catalyzes the reduction of hydrogen peroxide and some organic hydroperoxides by glutathione (GSH) and protects lipid membranes and other cellular components against oxidative stress, which is related to many diseases and this enzyme is regarded as one of the most important antioxidant enzymes in living organisms. Because the natural GPx has some shortcomings (e.g. instability and poor availability), scientists have paid more attention to its artificial imitation. Synthetic organoselenium and organotellurium compounds have emerged as excellent candidates to act as GPx mimics. Thus, in this study, several aminoacids derivatives containing selenium or tellurium were tested in order to evaluate their in vitro (i) GPx mimic properties (or GPx like activity) according to the model reaction (H202 + 2PhSH PhSSPh + 2H20); (ii) catalytic properties, (iii) reactivity with low molecular weight thiols (reduced glutathione, captopril and dithiothreitol) and (iv) their effect against lipid peroxidation have been performed. All compounds tested in this study showed ability to imitate de antioxidant enzyme GPx, but this property showed a dependence on the aminoacid residue and steric effect. Compounds C, D and 7g derivatives were found as the best catalysts in reducing peroxides, in comparison with other compounds tested. These results suggest that aminoacids derivatives compounds containing selenium or tellurium used in this work can be considered promising GPx mimetics.

A Glutationa Peroxidase (GPx; EC 1.11.1.9) é uma selenoenzima que catalisa a redução do peróxido de hidrogênio e hidroperóxidos orgânicos na presença de glutationa (GSH). Sua ação catalítica evita, desta forma, a oxidação dos lipídios constituintes da membrana, bem como de outros componentes celulares. Sabe-se que a produção excessiva de espécies reativas de oxigênio (EROs) está relacionada ao surgimento de muitas doenças, e a enzima GPx é considerada uma das mais importantes enzimas antioxidantes presentes nos organismos vivos, sendo necessária para auxiliar na proteção contra estas patologias. No entanto, a enzima GPx possui algumas desvantagens tais como, instabilidade e pouca viabilidade no que diz respeito a uma possível administração oral ou endovenosa, por isso, surgiu o interesse na síntese de compostos que possam mimetizar o mecanismo de ação dessa enzima. Dados da literatura têm demonstrado que os compostos orgânicos sintéticos de selênio (Se) e telúrio (Te) são excelentes miméticos da enzima GPx. Assim, neste estudo, uma série de compostos orgânicos derivados de aminoácidos contendo Se e Te na estrutura foram testados com a finalidade de avaliação in vitro da (i) atividade mimética da GPx (ou tipo GPx, isto é, GPx like activity) de acordo com a reação H2O2 + 2PhSH PhSSPh + 2H2O; (ii) propriedades catalíticas destes compostos, (iii) reatividade e possível oxidação dos compostos tiólicos de baixo peso molecular (glutationa reduzida, captopril e ditiotreitol) e o (iv) efeito…

Advisors/Committee Members: Helmoz Roseniaim Appelt, Roselei Fachinetto, João Batista Teixeira da Rocha, Maria Rosa Chitolina Schetinger.

Subjects/Keywords: organoselênio; Glutationa peroxidase; BIOQUIMICA; Glutathione peroxidase; organoselenium; organotellurium; organotelúrio

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APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6^th Edition):

Sudati, J. H. (2009). TOXICOLOGIA E FARMACOLOGIA IN VITRO DE NOVOS COMPOSTOS ORGÂNICOS DE SELÊNIO E TELÚRIO COM ATIVIDADE TIPO TIOL PEROXIDASE. (Thesis). Universidade Federal de Santa Maria. Retrieved from http://coralx.ufsm.br/tede/tde_busca/arquivo.php?codArquivo=2588

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Chicago Manual of Style (16^th Edition):

Sudati, Jessie Haigert. “TOXICOLOGIA E FARMACOLOGIA IN VITRO DE NOVOS COMPOSTOS ORGÂNICOS DE SELÊNIO E TELÚRIO COM ATIVIDADE TIPO TIOL PEROXIDASE.” 2009. Thesis, Universidade Federal de Santa Maria. Accessed April 17, 2021. http://coralx.ufsm.br/tede/tde_busca/arquivo.php?codArquivo=2588.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

MLA Handbook (7^th Edition):

Sudati, Jessie Haigert. “TOXICOLOGIA E FARMACOLOGIA IN VITRO DE NOVOS COMPOSTOS ORGÂNICOS DE SELÊNIO E TELÚRIO COM ATIVIDADE TIPO TIOL PEROXIDASE.” 2009. Web. 17 Apr 2021.

Vancouver:

Sudati JH. TOXICOLOGIA E FARMACOLOGIA IN VITRO DE NOVOS COMPOSTOS ORGÂNICOS DE SELÊNIO E TELÚRIO COM ATIVIDADE TIPO TIOL PEROXIDASE. [Internet] [Thesis]. Universidade Federal de Santa Maria; 2009. [cited 2021 Apr 17]. Available from: http://coralx.ufsm.br/tede/tde_busca/arquivo.php?codArquivo=2588.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Council of Science Editors:

Sudati JH. TOXICOLOGIA E FARMACOLOGIA IN VITRO DE NOVOS COMPOSTOS ORGÂNICOS DE SELÊNIO E TELÚRIO COM ATIVIDADE TIPO TIOL PEROXIDASE. [Thesis]. Universidade Federal de Santa Maria; 2009. Available from: http://coralx.ufsm.br/tede/tde_busca/arquivo.php?codArquivo=2588

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

29. Silva, Dianny Carolyne Vasconcelos da. Seleção de fungos de sedimento do rio Capibaribe contaminado com efluentes têxteis quanto à capacidade de produzir enzimas do complexo fenoloxidase e de descolorir corantes.

Degree: 2012, Universidade Federal de Pernambuco

URL: https://repositorio.ufpe.br/handle/123456789/10364

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FACEPE

Os efluentes têxteis contêm grandes quantidades de corantes, que quando lançados no ambiente representam riscos ecológico e de saúde pública, pois são tóxicos à… (more)

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FACEPE

Os efluentes têxteis contêm grandes quantidades de corantes, que quando lançados no ambiente representam riscos ecológico e de saúde pública, pois são tóxicos à vida aquática e são agentes mutagênicos, carcinogênicos e/ou teratogênicos. Os objetivos deste trabalho foram isolar e identificar fungos filamentosos de sedimento do Rio Capibaribe contaminado com efluentes de lavanderias industriais têxteis e selecionar fungos eficientes na produção de enzimas lignolíticas (manganês peroxidase, lignina peroxidase e lacase) e na descoloração de corantes sintéticos. As coletas do sedimento contaminado com efluentes das indústrias têxteis foram realizadas no município de Toritama-PE. Os fungos filamentosos foram isolados, identificados e selecionados em meio sólido quanto à produção de fenoloxidase. Os fungos selecionados foram analisados quanto à descoloração dos corantes têxteis Índigo Carmine, Azul Brilhante de Remazol e Vermelho Congo e a produção de manganês peroxidase, lignina peroxidase e lacase. Foram isoladas 31 espécies de fungos filamentosos. Os gêneros predominantes foram respectivamente: Aspergillus, Trichoderma e Penicillium. Quanto à seleção dos fungos filamentosos produtores de fenoloxidases, dos 49 isolados testados 18 demonstraram potencial para a produção da enzima. Fusarium redolens, Westerdykella dispersa, Aspergillus terreus I foram as espécies que demonstraram os maiores valores para a atividade de manganês peroxidase. Para a produção de lignina peroxidase o melhor produtor foi Aspergillus terreus II. Entre os produtores de lacase, Aspergillus terreus I e Aspergillus terreus III demontraram os melhores resultados. Quanto à descoloração dos corantes têxteis, Trichoderma hamatum II e Aspergillus terreus II apresentaram absorbância igual a zero ao longo de todo o espectro. Os resultados constataram que fungos filamentosos isolados de sedimento contaminado são eficientes na descoloração de corantes industriais têxteis e na produção de enzimas lignolíticas.

Advisors/Committee Members: Motta, Cristina Maria de Souza, Moreira, Keila Aparecida.

Subjects/Keywords: Fungos filamentosos; Corantes têxteis; Manganês peroxidase; Lignina peroxidase; Lacase

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APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6^th Edition):

Silva, D. C. V. d. (2012). Seleção de fungos de sedimento do rio Capibaribe contaminado com efluentes têxteis quanto à capacidade de produzir enzimas do complexo fenoloxidase e de descolorir corantes. (Masters Thesis). Universidade Federal de Pernambuco. Retrieved from https://repositorio.ufpe.br/handle/123456789/10364

Chicago Manual of Style (16^th Edition):

Silva, Dianny Carolyne Vasconcelos da. “Seleção de fungos de sedimento do rio Capibaribe contaminado com efluentes têxteis quanto à capacidade de produzir enzimas do complexo fenoloxidase e de descolorir corantes.” 2012. Masters Thesis, Universidade Federal de Pernambuco. Accessed April 17, 2021. https://repositorio.ufpe.br/handle/123456789/10364.

MLA Handbook (7^th Edition):

Silva, Dianny Carolyne Vasconcelos da. “Seleção de fungos de sedimento do rio Capibaribe contaminado com efluentes têxteis quanto à capacidade de produzir enzimas do complexo fenoloxidase e de descolorir corantes.” 2012. Web. 17 Apr 2021.

Vancouver:

Silva DCVd. Seleção de fungos de sedimento do rio Capibaribe contaminado com efluentes têxteis quanto à capacidade de produzir enzimas do complexo fenoloxidase e de descolorir corantes. [Internet] [Masters thesis]. Universidade Federal de Pernambuco; 2012. [cited 2021 Apr 17]. Available from: https://repositorio.ufpe.br/handle/123456789/10364.

Council of Science Editors:

Silva DCVd. Seleção de fungos de sedimento do rio Capibaribe contaminado com efluentes têxteis quanto à capacidade de produzir enzimas do complexo fenoloxidase e de descolorir corantes. [Masters Thesis]. Universidade Federal de Pernambuco; 2012. Available from: https://repositorio.ufpe.br/handle/123456789/10364

30. Tânia Regina de Assis. Obtenção de enzimas lignolíticas visando à hidrólise enzimática da fração lignocelulósica de bagaço de cana pré-tratado hidrotermicamente.

Degree: 2015, University of São Paulo

URL: http://www.teses.usp.br/teses/disponiveis/11/11138/tde-06012016-110640/

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A vinhaça e o bagaço de cana são os principais subprodutos oriundos do processamento da cana-de-açúcar nas indústrias sucroalcooleiras, sendo geradas grandes quantidades dos mesmos.… (more)

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A vinhaça e o bagaço de cana são os principais subprodutos oriundos do processamento da cana-de-açúcar nas indústrias sucroalcooleiras, sendo geradas grandes quantidades dos mesmos. O fungo basidiomiceto Pleurotus ostreatus tem a capacidade de degradar materiais lignocelulolíticos e produzir enzimas lignolíticas de interesse para as indústrias. Com o objetivo de avaliar a produção das enzimas lacases e peroxidase, o fungo Pleurotus ostreatus, foi cultivado em meio contendo bagaço pré-tratado e vinhaça, ou em meio contendo apenas vinhaça, em sistema de fermentação semissólido ou submerso; as enzimas extracelulares foram avaliadas após 7, 10 e 12 dias de cultivo. O bagaço peneirado foi considerado pré-tratado fisicamente (T1); para o pré-tratamento T2 o bagaço umedecido foi submetido a autoclave (121°C e 1 atm por 15 min); nos pré-tratamentos químicos, T3 e T4, o bagaço foi tratado com peróxido de hidrogênio e hidróxido de sódio nas seguintes concentrações: 0,75% H2O2 + 0,75% NaOH (T3) e 0,75% H2O2 + 1% NaOH (T4) na proporção 1:10 (p/v) e, em seguida foram submetidos à autoclave (121°C e 1 atm por 15min). A vinhaça utilizada foi proveniente de uma indústria sucroalcooleira (V1) e outra de destilaria (V2); a composição físico-química mostrou que a primeira possuía os índices de matéria orgânica e fósforo mais elevados que na vinhaça V2, enquanto que a relação C:N foi menor na vinhaça V1. Os extratos enzimáticos foram obtidos após filtração do meio submerso; para o meio semissólido foi necessário a adição de tampão citrato (1:5 p/v) antes da filtração. A atividade de lacasse e peroxidase em meio submerso, nos tratamentos com a vinhaça V1, foi superior ao observado em meio semissólido. A produção das enzimas em fermentação submersa, utilizando a vinhaça V1, apresentou valores de atividade de lacase, no tratamento TL1 e TL2, de 784,9 e 707,5 U.L-1, com atividade específica de 3,04 e 2,86 U.mg-1, respectivamente, e a amostra VL1, contendo apenas vinhaça, de 1,91 U.mg-1, no 12º dia de fermentação. Os valores mais altos de atividade de peroxidase foram obtidos nos tratamentos TL1, TL2, VL1, com 133,1; 131,2 e 126,1 U.L-1, respectivamente, após 12 dias de cultivo. A maior atividade específica obtida foi na VL1 (0,86 U.mg-1) no 7º dia de cultivo. O pré-tratamento físico do bagaço mostrou melhores condições para a produção das enzimas. Para a produção da lacase e da peroxidase é fundamental a composição da vinhaça.

The vinasse and bagasse are the principal by-products derived from the processing of sugarcane in the sugarcane industry, which generated large amounts of them. The basidiomycete fungus Pleurotus ostreatus, has the ability to degrade lignocellulolytic materials and produce lignolíticas enzymes of interest to industry. In order to evaluate the production of laccase and peroxidase enzymes, fungus P. ostreatus was grown in medium containing pre-treated bagasse and vinasse, or in medium containing only vinasse in semi-solid or submerged fermentation system; extracellular enzymes were evaluated after 7, 10 and…

Advisors/Committee Members: Sandra Helena da Cruz, Eliana Setsuko Kamimura, Rubens Monti.

Subjects/Keywords: Fungo; Lacase; Peroxidase; Vinhaça; Fungus; Laccase; Peroxidase; Vinasse

Record Details Similar Records Cite « Share

❌

APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6^th Edition):

Assis, T. R. d. (2015). Obtenção de enzimas lignolíticas visando à hidrólise enzimática da fração lignocelulósica de bagaço de cana pré-tratado hidrotermicamente. (Masters Thesis). University of São Paulo. Retrieved from http://www.teses.usp.br/teses/disponiveis/11/11138/tde-06012016-110640/

Chicago Manual of Style (16^th Edition):

Assis, Tânia Regina de. “Obtenção de enzimas lignolíticas visando à hidrólise enzimática da fração lignocelulósica de bagaço de cana pré-tratado hidrotermicamente.” 2015. Masters Thesis, University of São Paulo. Accessed April 17, 2021. http://www.teses.usp.br/teses/disponiveis/11/11138/tde-06012016-110640/.

MLA Handbook (7^th Edition):

Assis, Tânia Regina de. “Obtenção de enzimas lignolíticas visando à hidrólise enzimática da fração lignocelulósica de bagaço de cana pré-tratado hidrotermicamente.” 2015. Web. 17 Apr 2021.

Vancouver:

Assis TRd. Obtenção de enzimas lignolíticas visando à hidrólise enzimática da fração lignocelulósica de bagaço de cana pré-tratado hidrotermicamente. [Internet] [Masters thesis]. University of São Paulo; 2015. [cited 2021 Apr 17]. Available from: http://www.teses.usp.br/teses/disponiveis/11/11138/tde-06012016-110640/.

Council of Science Editors:

Assis TRd. Obtenção de enzimas lignolíticas visando à hidrólise enzimática da fração lignocelulósica de bagaço de cana pré-tratado hidrotermicamente. [Masters Thesis]. University of São Paulo; 2015. Available from: http://www.teses.usp.br/teses/disponiveis/11/11138/tde-06012016-110640/

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