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Study on the mechanism of mulberry polyphenols inhibiting oxidation of beef myofibrillar protein

文献类型： 外文期刊

作者： Huang, Xiang 1 ; Sun, Lu 1 ; Liu, Lan 1 ; Wang, Guoze 1 ; Luo, Peng 1 ; Tang, Daobang 2 ; Huang, Qun 1 ;

作者机构： 1.Guizhou Med Univ, Sch Publ Hlth, Key Lab Environm Pollut Monitoring & Dis Control, Minist Educ, Guiyang 550025, Peoples R China

2.Guangdong Acad Agr Sci, Sericultural & Agrifood Res Inst, Key Lab Funct Foods, Minist Agr & Rural,Affairs,Guangdong Key Lab Agr, Guangzhou 510610, Guangdong, Peoples R China

3.Chengdu Univ, Sch Food & Biol Engn, Meat Proc Key Lab Sichuan Prov, Chengdu 610106, Sichuan, Peoples R China

关键词： Mulberry polyphenols; Myofibrillar protein; Microstructure; Physicochemical properties; Oxidation system

期刊名称：FOOD CHEMISTRY （ 影响因子：9.231； 五年影响因子：8.795 ）

ISSN： 0308-8146

年卷期： 2022 年 372 卷

页码：

收录情况： SCI

摘要： In order to explore the mechanism of mulberry polyphenols inhibiting the oxidation of myofibrillar protein (MP), the effect of mulberry polyphenols on the structure and physicochemical properties of MP in the oxidation system was investigated. The results revealed that the content of carbonyl group and sulfhydryl group of MP was notably reduced, while the Zeta potential, storage modulus G' and surface hydrophobicity were improved when the addition of mulberry polyphenol was 0.5%. SDS-PAGE showed an irreducible aggregation of mulberry polyphenols with proteins. Fluorescence spectroscopy and FT-IR analysis manifested that mulberry polyphenols promoted the unfolding of protein structure and the transformation of alpha-helix to beta-turn structure. Scanning electron microscopy (SEM) observed that oxidation with polyphenols facilitated the cross-linking and aggregation of MP more tightly. Nevertheless, excessive addition (>= 1.0%) weakened its gel properties. Thus, to maintain the good quality of meat products, both polyphenols addition and oxidation intensity should be controlled simultaneously.

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