Effects of oxidative modification on textural properties and gel structure of pork myofibrillar proteins
文献类型： 外文期刊
作者： Xia, Minquan 1 ; Chen, Yinxia 2 ; Guo, Juanjuan 1 ; Feng, Xiaolong 1 ; Yin, Xiaoli 1 ; Wang, Lan 4 ; Wu, Wenjin 4 ; Li, Z 1 ;
作者机构： 1.Yangtze Univ, Coll Life Sci, Jingzhou 434023, Hubei, Peoples R China
2.Huazhong Agr Univ, Coll Food Sci & Technol, Wuhan 430070, Hubei, Peoples R China
3.Yangtze Univ, Jingchu Food Res & Dev Ctr, Jingzhou 434023, Hubei, Peoples R China
4.Hubei Acad Agr Sci, Inst Farm Prod Proc & Nucl Agr Technol, Wuhan 430064, Hubei, Peoples R China
关键词： Protein oxidation; Gel properties; T-2 Relaxation time; Raman spectroscopy
期刊名称：FOOD RESEARCH INTERNATIONAL （ 影响因子：6.475； 五年影响因子：6.508 ）
ISSN： 0963-9969
年卷期： 2019 年 121 卷
页码：
收录情况： SCI
摘要： Isolated myofibrillar protein (MP) was treated by the oxidation system of FeCl3 (0.01 mM) at four different H2O2 concentrations (0, 1, 10, 20 mM). The oxidation degree was determined by measuring the carbonyl and total sulphydryl values. The structure and physicochemical properties of MP gels were investigated by water holding capacity (WHC) evaluation, sodium dodecyl sulfate-polyacryl amide gel electrophoresis (SDS-PAGE), texture profile analysis (TPA), Raman spectroscopy, and NMR transverse relaxation (T-2). The results of carbonyls and total sulphydryls indicated that oxidation degree of MP increased with increasing H2O2 concentration. TPA showed that moderate oxidation (10 mM H2O2) could improve the hardness, springiness, gumminess and cohesiveness of MP gels, but not contribute to the maintenance of their WHC, probably due to severe depolymerization of MPs, unfolding of alpha-helix, exposure of the hydrophobic groups and the migration of protein-associated water (T-2b) and intra-myofibrillar water (T-21) to the longer relaxation time.
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