Effects of iron-catalyzed oxidation and methemoglobin oxidation systems on endogenous enzyme activity and myofibrillar protein degradation in yak meat

被引：23

作者：

Bu, Xinrong ^{[1
]}

Wang, Huihui ^{[1
]}

Wang, Yujiao ^{[1
]}

Ojangba, Theodora ^{[1
]}

Nan, Huaili ^{[1
]}

Zhang, Li ^{[1
]}

Yu, Qunli ^{[1
]}

机构：

[1] Gansu Agr Univ, Coll Food Sci & Engn, Lanzhou 730070, Peoples R China

来源：

FOOD CHEMISTRY | 2023年 / 404卷

基金：

中国国家自然科学基金;

关键词：

Iron -catalyzed oxidation system; Methemoglobin oxidation system; Endogenous enzymes; Degradation of myofibrillar proteins; MU-CALPAIN; SKELETAL-MUSCLE; CROSS-LINKING; TENDERNESS; CASPASE-3; SUSCEPTIBILITY; PROTEOLYSIS; ACTIVATION; MYOGLOBIN; CAPACITY;

D O I：

10.1016/j.foodchem.2022.134647

中图分类号：

O69 [应用化学];

学科分类号：

081704 ;

摘要：

In this study, the effects of different oxidation intensities on the degradation of myofibrillar protein by endogenous enzymes in iron-catalyzed oxidizing (IOS) and metmyoglobin oxidizing system (MOS) were compared. The results showed that carbonyl content and endogenous enzyme activities (caspase-3, caspase-6 and calpain-1) increased significantly and the total sulfhydryl content decreased significantly with H2O2 concentration in both oxidation systems. Meanwhile, the rate of carbonyl formation and the inhibition of endogenous enzymes activities of IOS were significantly lower than MOS for the same oxidation intensity. In addition, IOS and MOS mainly produced myosin light chains degradation products of 20-25 kDa and 20-17 kDa. At the same oxidation intensity, MOS of myofibrillar protein significantly enhanced the degradation of troponin-T and desmin by caspase-3/-6 compared with IOS, while inhibiting the degradation of troponin-T by calpain-1. In conclusion, MOS inhibited endogenous enzyme degradation in vitro more than IOS during post-slaughter maturation of yak meat.

引用

页数：14

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