鸭梨果实多酚氧化酶酶学特性  

Characterization of Polyphenol Oxidase from Yali Pear

作　　者：李健[1] 徐艳聪[1] 黄美[2] 杨洋[2] 曹建康[2] 姜微波[2] 

机构地区：[1]北京工商大学食品学院,北京市食品风味化学重点实验室,食品添加剂与配料北京高等学校工程研究中心,北京100048 [2]中国农业大学食品科学与营养工程学院,北京100083

出　　处：《食品科学》2013年第15期154-157,共4页Food Science

基　　金：国家自然科学基金项目(31201431)

摘　　要：从鸭梨果实中提取多酚氧化酶(PPO),以邻苯二酚为底物,采用分光光度法研究pH值、温度、抑制剂及激活剂对其活性的影响。结果表明:鸭梨果实PPO在pH4.0～6.0时活性较高,在80℃时,热稳定性较差。浓度为0.5mmol/L的抗坏血酸和L-半胱氨酸对PPO活性的抑制率分别为96.8%和98.3%,几乎可以完全抑制PPO酶活性;浓度为25mmol/L的十二烷基磺酸钠(SDS)可以使鸭梨果实PPO活性增强435%,氯化铜同样可以激活PPO活性。Polyphenol oxidase （PPO） was extracted from Yali pear, and the effects of pH, temperature, activator, and inhibitor on its activity were explored by spectroscopy. The PPO showed high activity at pH 4.0 to 6.0. Heat inactivation studies showed a rapid decrease in enzyme activity at 80 ℃. Its activity was inhibited by 96.8% and 98.3% in the presence of 0.5 mmol/L ascorbic acid and L-cysteine, respectively. In addition, the enzyme activity was enhanced by sodium dodecyl sulfate （by 435%） and CuCl2.

关 键 词：鸭梨 多酚氧化酶 抑制剂 激活剂 

分 类 号：TS255.1[轻工技术与工程—农产品加工及贮藏工程]