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Enzymatic Properties of Polyphenol Oxidase from Kuerle Pear

Tingting Du

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Abstract

Enzymological characterization of the polyphenol oxidase(PPO) from Kuerle pear towards catechol as a substrate was conducted using spectrophotometry method.The results showed that the optimal pH and temperature for this enzyme was 5.7 and 42 ℃.High temperature treatment could inhibit PPO activity.The kinetics of PPO reaction was in accord with the Michaelis-Menten equation,with Km and Vmax values of 0.152 mol/L and 169.49 U/min,respectively.Ascorbic acid exhibited stronger inhibition effect on PPO activity than citric acid,NaCl and EDTA-2Na.

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What this paper is about

Enzymological characterization of the polyphenol oxidase(PPO) from Kuerle pear towards catechol as a substrate was conducted using spectrophotometry method.The results showed that the optimal pH and temperature for this enzyme was 5.7 and 42 ℃.High temperature treatment could inhibit PPO activity.The kinetics of PPO reaction was in accord with the Michaelis-Menten equation,with Km and Vmax values of 0.152 mol/L and 169.49 U/min,respectively.Ascorbic acid exhibited stronger inhibition effect on PPO activity than citric acid,NaCl and EDTA-2Na.

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Available abstract

Enzymological characterization of the polyphenol oxidase(PPO) from Kuerle pear towards catechol as a substrate was conducted using spectrophotometry method.The results showed that the optimal pH and temperature for this enzyme was 5.7 and 42 ℃.High temperature treatment could inhibit PPO activity.The kinetics of PPO reaction was in accord with the Michaelis-Menten equation,with Km and Vmax values of 0.152 mol/L and 169.49 U/min,respectively.Ascorbic acid exhibited stronger inhibition effect on PPO activity than citric acid,NaCl and EDTA-2Na.

Key concepts: Polyphenol oxidase, PEAR, Chemistry, Ascorbic acid, Catechol, Enzyme, Substrate (aquarium), Citric acid

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