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Biochemical properties of oxidases of Yali pear

机译：亚利梨氧化酶的生化特性

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The biochemical properties of polyphenol oxidase (PPO), peroxidase (POD) andascorbate peroxidase?(APX) from Yali pear were investigated. The optimum pH and temperature of three enzymes was 5.6, 4.0, 7.0 and 20, 40, 50°C, respectively. Enzyme kinetics results showed that the Michaelis constant (Km) and maximum velocity (Vmax) of PPO for catechol were 0.22 M and 1111 U/ml/min. The Km and Vmax values of POD for guaiacol were 0.14 M and 1429 U/ml/min. The Km of APX for ascorbic acid and H2O2?were 0.41 and 0.083 mM, respectively, and the Vmax of APX was 455 and 208 U/ml/min for ascorbic acid and H2O2, respectively. The inhibitory effects of the four inhibitors (ascorbic acid, citric acid, L-cysteine and phytic acid) on each enzyme were different, suggesting that the composite inhibitor is more appropriate for processing of Yali pear.
机译：研究了来自亚利梨的多酚氧化酶（PPO），过氧化物酶（POD）的生物化学性质，过氧化物酶过氧化物酶？（APX）。三种酶的最佳pH和温度分别为5.6,4.0,7.0和20,40,50℃。酶动力学结果表明，儿茶酚PPO的Michaelis常数（km）和最大速度（Vmax）为0.22m和1111 u / ml / min。 POD的KM和VMAX值为Guaiacol为0.14m和1429 U / ml / min。抗坏血酸和H 2 O 2的APX的KM分别为0.41和0.083mm，APX的VMAX分别用于抗坏血酸和H2O2的455和208U / ml / min。四种抑制剂（抗坏血酸，柠檬酸，L-半胱氨酸和植物酸）对每种酶的抑制作用不同，表明复合抑制剂更适合加工亚利梨。

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