Journal Article10.1016/J.FOODCHEM.2017.07.028
Importance of salt and temperature in myosin polymerization during surimi gelation.
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TL;DR: In gel samples made without salt, no myosin heavy chain (MHC) polymerization was observed, only aggregation, but in gels made with added salt, MHC polymerization occurred, as evidenced by the electrophoresis, and the gelation resulted in a well-stabilized protein network with good physicochemical properties.
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About: This article is published in Food Chemistry. The article was published on 15 Jan 2018. The article focuses on the topics: Polymerization & Agarose.
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Citations
Role of Cryoprotectants in Surimi and Factors Affecting Surimi Gel Properties: A Review
Noman Walayat,Hanguo Xiong,Zhouyi Xiong,Helena M. Moreno,Asad Nawaz,Nadia Niaz,Muhammad Atif Randhawa +6 more
TL;DR: In this article, a good source of myofibrillar proteins, stabilized with the addition of cryoprotectants during long-term frozen storage, was found to be effective in protecting phys...
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Insight into the mechanism of textural deterioration of myofibrillar protein gels at high temperature conditions.
TL;DR: High temperature-induced textural deterioration of MP gel was initialized by the dramatic changes of protein structures during heat treatment, which decreased thermal stability of MP gels due to the over-aggregation of MP molecules.
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Microwave irradiation promotes aggregation behavior of myosin through conformation changes
Hongwei Cao,Xidong Jiao,Daming Fan,Jianlian Huang,Jianxin Zhao,Bowen Yan,Wenguo Zhou,Hao Zhang,Mingfu Wang +8 more
TL;DR: In this paper, the role of microwave on myosin aggregation during different heating processes was investigated and the potential relationship between conformation changes and physicochemical properties of myosins was explored.
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Myofibrillar protein conformation enhance gel properties of mixed surimi gels with Nemipterus virgatus and Hypophthalmichthys molitrix
Shumin Yi,Li Qiang,Cuiping Qiao,Zhang Chang,Wang Wei,Yongxia Xu,Hongbo Mi,Xuepeng Li,Jianrong Li +8 more
TL;DR: In this article, the authors investigated changing in myofibrillar protein conformation enhance the properties of mixed surimi gels formed by thermal processing and obtained results that heating increases the fracture constant of the 3:1 and 1:5 surimi mixtures.
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Gelation properties and thermal gelling mechanism of golden threadfin bream myosin containing CaCl2 induced by high pressure processing
TL;DR: The effects and mechanism of high-pressure processing (HPP) and CaCl2 addition on golden threadfin bream myosin gel were investigated in this article, which revealed that HPP at 100-300MPa could markedly improve the gelation properties.
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