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Effects of oxidative modification on textural properties and gel structure of pork myofibrillar proteins.

Authors
  • Xia, Minquan1
  • Chen, Yinxia2
  • Guo, Juanjuan1
  • Feng, Xiaolong1
  • Yin, Xiaoli1
  • Wang, Lan3
  • Wu, Wenjin3
  • Li, Zhenshun4
  • Sun, Weiqing5
  • Ma, Jing4
  • 1 College of Life Science, Yangtze University, Jingzhou, Hubei 434023, PR China. , (China)
  • 2 College of Food Science and Technology, Huazhong Agricultural University, Wuhan, Hubei 430070, PR China. , (China)
  • 3 Hubei Academy of Agricultural Science, Institute for Farm Products Processing and Nuclear-Agricultural Technology, Wuhan, Hubei 430064, PR China. , (China)
  • 4 College of Life Science, Yangtze University, Jingzhou, Hubei 434023, PR China; Jingchu Food Research and Development Center, Yangtze University, Jingzhou, Hubei 434023, PR China. , (China)
  • 5 College of Life Science, Yangtze University, Jingzhou, Hubei 434023, PR China; Jingchu Food Research and Development Center, Yangtze University, Jingzhou, Hubei 434023, PR China. Electronic address: [email protected] , (China)
Type
Published Article
Journal
Food research international (Ottawa, Ont.)
Publication Date
Jul 01, 2019
Volume
121
Pages
678–683
Identifiers
DOI: 10.1016/j.foodres.2018.12.037
PMID: 31108795
Source
Medline
Keywords
Language
English
License
Unknown

Abstract

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 (T2). 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 α-helix, exposure of the hydrophobic groups and the migration of protein-associated water (T2b) and intra-myofibrillar water (T21) to the longer relaxation time. Copyright © 2019 Elsevier Ltd. All rights reserved.

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