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化学抑制剂对果蔬食品多酚氧化酶性质影响的研究进展

  • 周亨乐 ,
  • 王富海 ,
  • 易俊洁 ,
  • 程冯云 ,
  • 袁蕾 ,
  • 牛慧慧 ,
  • 周林燕
展开
  • (昆明理工大学 农业与食品学院,云南 昆明, 650500)
硕士研究生(周林燕副教授为通讯作者,E-mail:zhoulinyan916@hotmail.com)

收稿日期: 2020-06-09

  修回日期: 2020-09-07

  网络出版日期: 2021-03-16

基金资助

国家自然科学基金项目(31860445)

Research progress on the effect of chemical inhibitors on the properties of polyphenol oxidase in fruits and vegetables

  • ZHOU Hengle ,
  • WANG Fuhai ,
  • YI Junjie ,
  • CHENG Fengyun ,
  • YUAN Lei ,
  • NIU Huihui ,
  • ZHOU Linyan
Expand
  • (Faculty of Agriculture and Food, Kunming University of Science and Technology, Kunming 650500, China)

Received date: 2020-06-09

  Revised date: 2020-09-07

  Online published: 2021-03-16

摘要

多酚氧化酶(polyphenol oxidase, PPO)引起的酶促褐变会导致果蔬食品色泽劣变,营养成分降低,甚至使其丧失商品价值。化学抑制剂对PPO具有较好的抑制效果,并且使用方便,在果蔬食品中广泛使用,因此对它的研究具有理论和实际意义。该文论述了羧酸、抗坏血酸及其衍生物、含硫氨基酸、酚酸及其他抑制剂对PPO的抑制作用和机理,并分析了它们在食品工业应用中的优缺点。同时,从分子水平上探讨了化学抑制剂处理后PPO构象变化,以及抑制剂与 PPO的相互作用方式,得出了化学抑制剂可通过强酸作用、螯合作用、还原作用和强结合作用来导致PPO构象变化而抑制酶活,为深入研究抑制剂对PPO的抑制机理提供了理论参考。

本文引用格式

周亨乐 , 王富海 , 易俊洁 , 程冯云 , 袁蕾 , 牛慧慧 , 周林燕 . 化学抑制剂对果蔬食品多酚氧化酶性质影响的研究进展[J]. 食品与发酵工业, 2021 , 47(4) : 253 -260 . DOI: 10.13995/j.cnki.11-1802/ts.024661

Abstract

Enzymatic browning caused by polyphenol oxidase (PPO) lead to color deterioration of fruit and vegetable products, reduction of nutritional components, and even loss of commercial value. Chemical inhibitors show good inhibition effect on PPO, and are easy to use. They are widely used in fruit and vegetable products, thus its research has theoretical and practical significance. The inhibition and mechanism of carboxylic acid, ascorbic acid and its derivatives, sulfur-containing amino acid, phenolic acid and other inhibitors on PPO were discussed, and their advantages and disadvantages in the application of food industry were analyzed. At the same time, the conformational changes of PPO treated by chemical inhibitors and the interaction mode between these inhibitors and PPO were discussed at the molecular level. It was concluded that chemical inhibitors can inhibit enzyme activity through strong acid action, chelation, reduction and strong binding cooperation, which provides a theoretical reference for further study of the inhibition mechanism of inhibitors on PPO.

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