Glucose oxidase promotes gallic acid-myofibrillar protein interaction and thermal gelation

被引：55

作者：

Guo, Anqi ^{[1
]}

Xiong, Youling L. ^{[1
]}

机构：

[1] Univ Kentucky, Dept Anim & Food Sci, Lexington, KY 40546 USA

来源：

FOOD CHEMISTRY | 2019年 / 293卷

基金：

美国食品与农业研究所; 国家重点研发计划;

关键词：

Gallic acid; Myofibrillar protein; Glucose oxidase; Gelation; Meat; CROSS-LINKING; PHENOLIC-COMPOUNDS; GEL PROPERTIES; FLUORESCENCE; ENHANCEMENT; OXIDATION; MEAT; ANTIOXIDANT; PROOXIDANT; PRODUCTS;

D O I：

10.1016/j.foodchem.2019.05.018

中图分类号：

O69 [应用化学];

学科分类号：

081704 ;

摘要：

The effect of glucose oxidase (GOx) catalytic oxidation on the efficacy of gallic acid (GA) to modify the chemical structure and gelling behavior of myofibrillar protein (MP) was investigated. In contrast to non-oxidized MP samples where GA induced very little changes, GA (0, 6, 30, and 60 mu mol/g MP) under GOx treatment promoted sulfhydryl and amine loss (up to 58% and 49%, respectively). The attenuation of intrinsic tryptophan fluorescence in the GA/GOx-treated MP corroborated the finding. The gelling capacity of MP, corresponding to disulfide and non-disulfide bond formation in protein aggregates, was markedly enhanced by 60 mu mol GA under GOx, up to 86% in gel storage modulus G' and 53% in gel strength. The GOx-aided GA modification of MP could be a potential ingredient strategy in meat processing to promote textural attributes of cooked products.

引用

页码：529 / 536

页数：8

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