Exploring the regulating mechanism of heat induced gelation of myosin by binding with Mb hemin prosthetic group
文献类型： 外文期刊
作者： Zhu, Hongxing 1 ; Zhang, Muhan 1 ; Wang, Peng 2 ; Sun, Chong 1 ; Xu, Weimin 1 ; Ma, Jingjing 1 ; Zhu, Yongzhi 1 ; Wang, Daoying 1 ;
作者机构： 1.Jiangsu Acad Agr Sci, Inst Agr Prod Proc, Nanjing 210014, Peoples R China
2.Nanjing Agr Univ, Jiangsu Collaborat Innovat Ctr Meat Prod & Proc Q, Nanjing 210095, Peoples R China
3.Qinghai Prov Qinghai Lake Meat Ind Co Ltd, Qinghai 813000, Hainan, Peoples R China
关键词： Hemin prosthetic group; Myosin; Oxidation; Affinity; Regulating mechanism
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 382 卷
页码：
收录情况： SCI
摘要： The properties, structure and water holding capacity of myosin were analyzed after incubated with myoglobin (Mb) hemin prosthetic group. The results revealed moderate oxidation of hemin prosthetic group could improve the solubility of myosin. Besides, it could stretch the protein structure and cross-link the molecules to form the soluble polymer. Hence, moderate oxidation could improve the gel properties and the gel network structure. However, excessive oxidation would greatly reduce the physical and chemical properties of myosin, which was not conducive to the gel formation and would lead to a decrease in water retention. Moreover, fluorescence spectroscopy and cyclic voltammetry (CV) proved hemin prosthetic group had a high affinity for myosin. The interaction mechanism was further studied by molecular docking and molecular dynamics (MD) simulations. This study provides some fundamental prospects to be applied in the functional regulation of meat protein.
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