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- W2030804089 abstract "The monophenolase activity of quince pulp polyphenol oxidase was characterized by extracting samples using a combination of a two-phase partition step in Triton X-114, followed by a PEG 8000/phosphate partition step, and a final ammonium sulfate fractionation between 30 and 75%. The purification method avoids the loss of cresolase activity described in another quince pulp polyphenol oxidase. The activity was characterized by a lag period, whose duration depended on the substrate concentration, the pH, and the presence of catalytic amounts of o-diphenol. By increasing the concentration of o-diphenols, it was possible to evaluate the enzyme activation constant, K(act), which showed a value of 4.5 microM for 4-methylcatechol. A general kinetic mechanism for this enzyme is used to explain the loss of activity that normally occurs during quince pulp polyphenol oxidase purification." @default.
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- W2030804089 date "2005-01-22" @default.
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- W2030804089 title "A Kinetic Study of <i>p</i>-Cresol Oxidation by Quince Fruit Polyphenol Oxidase" @default.
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- W2030804089 doi "https://doi.org/10.1021/jf040080g" @default.
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