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Study on Reaction Kinetics Characteristics of Polyphenol Oxidase of Cryopreservation Fresh Tea Leaves

Xiaoqiang Chen

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Abstract

The polyphenol oxidase activity of cryopreservation fresh tea leaves was determined by spectrophotometric method.The influence of main factors,such as substrate concentration,system pH and temperature on catalytic activities of PPO were investigated.The results showed that,the optimum pH and temperature for the enzymatic reaction was 4.6~5.0 and 35~60 ℃,respectively.The Michaelis-Menten equation of PPO from cryopreservation fresh tea leaves was established,accordingly1/v=1.168 8/[S]+3.083 3,by which the kinetic parameters obtained were as follow: Km=0.378 mol/L,vmax=0.324 U /min.

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What this paper is about

The polyphenol oxidase activity of cryopreservation fresh tea leaves was determined by spectrophotometric method.The influence of main factors,such as substrate concentration,system pH and temperature on catalytic activities of PPO were investigated.The results showed that,the optimum pH and temperature for the enzymatic reaction was 4.6~5.0 and 35~60 ℃,respectively.The Michaelis-Menten equation of PPO from cryopreservation fresh tea leaves was established,accordingly1/v=1.168 8/[S]+3.083 3,by which the kinetic parameters obtained were as follow: Km=0.378 mol/L,vmax=0.324 U /min.

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Available abstract

The polyphenol oxidase activity of cryopreservation fresh tea leaves was determined by spectrophotometric method.The influence of main factors,such as substrate concentration,system pH and temperature on catalytic activities of PPO were investigated.The results showed that,the optimum pH and temperature for the enzymatic reaction was 4.6~5.0 and 35~60 ℃,respectively.The Michaelis-Menten equation of PPO from cryopreservation fresh tea leaves was established,accordingly1/v=1.168 8/[S]+3.083 3,by which the kinetic parameters obtained were as follow: Km=0.378 mol/L,vmax=0.324 U /min.

Key concepts: Polyphenol oxidase, Chemistry, Cryopreservation, Substrate (aquarium), Kinetics, Polyphenol, Food science, Enzyme

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