Results 181 to 190 of about 306,357 (240)
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ChemCatChem, 2013
Enzymatic mimics are designed by using small molecules to impart insight into the mechanistic pathways of the enzymes and to generate catalysts that could be as efficient as the enzyme itself. Among the copper-based polyphenol oxidase enzymes, the copper(II)-containing enzyme catechol oxidase catalyses exclusively the oxidation of ortho-diphenols to ...
Suman Kr Dey, Arindam Mukherjee
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Enzymatic mimics are designed by using small molecules to impart insight into the mechanistic pathways of the enzymes and to generate catalysts that could be as efficient as the enzyme itself. Among the copper-based polyphenol oxidase enzymes, the copper(II)-containing enzyme catechol oxidase catalyses exclusively the oxidation of ortho-diphenols to ...
Suman Kr Dey, Arindam Mukherjee
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Ag-doped CdO nanocatalysts: Preparation, characterization and catechol oxidase activity
Journal of Molecular Structure, 2018Silver doped cadmium oxide (Ag/CdO) nanoparticles with an average size of 41 nm have been successfully synthesized via thermal decomposition and liquid impregnation technique.
M. El-Kemary +2 more
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Evidence for conformational changes in grape catechol oxidase
Phytochemistry, 1972Abstract A rapid, 4–10-fold, activation of grape catechol oxidase by a short exposure to acid pH or urea is demonstrated. Activation was either reversible or irreversible, depending on length and type of treatment. The change in activity of the enzyme is due primarily to an increase in V max , while the affinity for 4-methylcatechol decreases and ...
H.R. Lerner, A.M. Mayer, E. Harel
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Isoelectric point changes in Vitis vinifera catechol oxidase
Phytochemistry, 1974Abstract A comparison between electrophoretic and isoelectric focussing patterns of grape catechol oxidase is reported.
M. Dubernet, null Ribéreau-Gayon
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Stokes' radius changes of solubilized grape catechol oxidase
Phytochemistry, 1975Abstract The Stokes' radius of grape catechol oxidase was determined at pH 7·0 and during its reversible and irreversible activation at pH 5·0. The results are consistent with the view that the activation is due to a conformational change in the enzyme.
H.R. Lerner, A.M. Mayer
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Enzymatic dynamics of catechol oxidase from Gastrolina depressa
Pesticide Biochemistry and Physiology, 2010Abstract Properties of the phenoloxidase (PO) from adult of Gastrolina depressa Baly (Coleoptera: Chrysomelidae) as well as effects of some metal ions and inhibitors on the activity of PO purified by (NH 4 ) 2 SO 4 were determined. The optimal pH and temperature of the enzyme for the oxidation of catechol were determined to be at pH 7.5 and at 40 °
Yan Zhao +4 more
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Tea catechol oxidase: Isolation, purification and kinetic characterization
Phytochemistry, 1973Abstract Cathechol oxidase extracted from tea leaves was purified over 200-fold, using isoelectric focusing. The purified catechol oxidase was free of peroxidase and flavanol gallate esterase activities. Further, this enzyme was shown to have optimum activity near pH 5·7 and a Km of 2·3 × 10−3 M (at 25°) for (−)-epigallocatechin gallate. The purified
Philip Coggon +2 more
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Phenylhydrazine, a specific irreversible inhibitor of catechol oxidase
Phytochemistry, 1971Abstract Phenylhydrazine is shown to specifically inhibit a number of catechol oxidases from plant tissues. A laccase-like enzyme from peaches is not inhibited while ascorbic oxidase is only partly inhibited by relatively high concentrations of the inhibitor.
H.R. Lerner +3 more
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Copper Based Biomimetic Catalysts of Catechol Oxidase: An Overview on Recent Trends
Catalysis in Industry, 2022Sahin Reja, Ambica Kejriwal, R. Das
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Catechol oxidase from green olives: Properties and partial purification
Phytochemistry, 1977Abstract Catechol oxidase was extracted from an acetone powder prepared from green olive. The enzyme was purified 240-fold by ammonium sulphate fractionation followed by ion exchange chromatography and gel filtration. The enzyme was characterized by substrate specificity and response to inhibitors.
Noach Ben-Shalom +3 more
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