Effect of in vitro oxidation on the water retention mechanism of myofibrillar proteins gel from pork muscles

被引：127

作者：

Zhang, Dong ^{[1
]}

Li, Hongjun ^{[1
,2
]}

Emara, A. M. ^{[1
]}

Hu, Ying ^{[1
]}

Wang, Zefu ^{[1
]}

Wang, Mengqi ^{[1
]}

He, Zhifei ^{[1
,2
]}

机构：

[1] Southwest Univ, Coll Food Sci, Chongqing 400715, Peoples R China

[2] Chongqing Engn Res Ctr Reg Food, Chongqing 400715, Peoples R China

来源：

FOOD CHEMISTRY | 2020年 / 315卷

基金：

国家重点研发计划;

关键词：

Oxidation; Pork; Myofibrillar proteins; Gel; Water holding capacity; HOLDING CAPACITY; CROSS-LINKING; GELATION PROPERTIES; STRUCTURAL-CHANGES; FROZEN STORAGE; MEAT; PRESSURE; MALONDIALDEHYDE; CARBONYLATION; CONFORMATION;

D O I：

10.1016/j.foodchem.2020.126226

中图分类号：

O69 [应用化学];

学科分类号：

081704 ;

摘要：

The aim of this study was to investigate the effects of oxidation on the structure of pork myofibrillar proteins (MPs) and the water retention mechanism of MPs gel. In a Fenton reaction system, protein oxidation increases (P < 0.05) with hydrogen peroxide (H2O2) concentration (0, 0.5, 1, 3, 5, 10, and 20 mmol/L). The Brunauer-Emmett-Teller surface area of the proteins gel gradually increased (P < 0.05) from 6.17 m(2)/g to 14.73 m(2)/g. Low field nuclear magnetic resonance results showed that immobilized water in the gel gradually decreased but free water content gradually increased (P < 0.05). Gel strength and water holding capacity (WHC) increased and then decreased. The results reveal that moderate oxidation contributes to the compact and uniform pore structure, higher WHC of proteins gel as well. However, excessive oxidation leads to increase pores and changes in water states of gel, leading to lower WHC.

引用

页数：8

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