Effect of peroxyl radicals on the structure and gel properties of isolated rabbit meat myofibrillar proteins

被引：91
作者：
Wang, Zhaoming [1 ,2 ]
He, Zhifei [1 ,2 ]
Gan, Xiao [1 ,2 ]
Li, Hongjun [1 ,2 ]
机构：
[1] Chongqing Engn Res Ctr Reg Food, Chongqing, Peoples R China
[2] Southwest Univ, Coll Food Sci, 2 Tiansheng Rd, Chongqing 400715, Peoples R China
来源：
INTERNATIONAL JOURNAL OF FOOD SCIENCE AND TECHNOLOGY | 2018年 / 53卷 / 12期
基金：
中国国家自然科学基金;
关键词：
Gel properties; myofibrillar proteins; peroxyl radicals; protein structure; rabbit meat; METAPENAEUS-ENSIS TROPOMYOSIN; FATTY-ACID-COMPOSITION; IGE BINDING-CAPACITY; OXIDATIVE MODIFICATION; SYSTEMS; BEEF; MECHANISMS; HYDROPHOBICITY; CONFORMATION; PRODUCTS;
D O I：
10.1111/ijfs.13878
中图分类号：
TS2 [食品工业];
学科分类号：
0832 ;
摘要：
We investigated the effect of peroxyl radicals (ROO center dot), which are products of lipid peroxidation, on the structure and gel properties of myofibrillar proteins (MPs) isolated from rabbit meat. 2,2 '-Azobis(2-amidinopropane) dihydrochloride (AAPH) was heated to stably derive ROO center dot. As the AAPH concentration increased, the protein carbonyl compounds significantly accumulated (P < 0.05), and the total sulfhydryl content was significantly lost (P < 0.05). Circular dichroism spectra, UV absorption spectra, intrinsic fluorescence spectra and surface hydrophobicity revealed that ROO center dot caused protein unfolding and conformational changes in MPs. Sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) analysis indicated that moderate (0-3 mm) and relatively high (5 and 10 mm) AAPH concentrations could lead to protein crosslinking and protein aggregation, respectively. These changes in protein structure could influence the gelling properties of MPs. Low-level protein oxidation could increase gel strength and water holding capacity, whereas high-level protein oxidation could reduce gel properties.
引用
收藏
页码：2687 / 2696
页数：10
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