摘要
以邻苯二酚为底物,采用分光光度法对库尔勒梨多酚氧化酶(PPO)的酶学特性进行研究。结果表明:库尔勒梨PPO的最适pH值为5.7,最适温度为42℃;短时间高温能显著抑制PPO酶活力;PPO催化的酶促褐变反应符合米氏动力学方程,该酶促反应的最大速率为169.49U/min,Km值为0.152mol/L;与柠檬酸、NaCl和EDTA-2Na相比,抗坏血酸对库尔勒梨PPO的抑制效果较好。
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.
出处
《食品科学》
EI
CAS
CSCD
北大核心
2010年第21期275-278,共4页
Food Science
基金
鲁东大学校基金项目(LY20063307)
鲁东大学学科建设经费资助项目
关键词
库尔勒梨
多酚氧化酶
酶学特性
抑制效应
Kuerle pear
polyphenol oxidase
enzymatic properties
inhibition effect
