Conformational changes induced by high-pressure homogenization inhibit myosin filament formation in low ionic strength solutions

被引:120
作者
Chen, Xing [1 ,2 ]
Xu, Xinglian [1 ,2 ]
Han, Minyi [1 ,2 ]
Zhou, Guanghong [1 ,2 ]
Chen, Conggui [3 ]
Li, Peijun [3 ]
机构
[1] Nanjing Agr Univ, Key Lab Meat Proc & Qual Control, Jiangsu Synerget Innovat Ctr Meat Prod & Proc, Key Lab Anim Prod Proc,Minist Agr,Minist Educ, Nanjing 210095, Jiangsu, Peoples R China
[2] Nanjing Agr Univ, Coll Food Sci & Technol, Nanjing 210095, Jiangsu, Peoples R China
[3] Hefei Univ Technol, Sch Biol & Food Engn, Hefei 230009, Anhui, Peoples R China
基金
中国国家自然科学基金;
关键词
Myofibrillar proteins; Myosin; High-pressure homogenization; Conformation; Solubility; Filament formation; MYOFIBRILLAR PROTEIN; SECONDARY STRUCTURES; PORCINE MYOSIN; CROSS-LINKING; L-HISTIDINE; MICROBIAL TRANSGLUTAMINASE; SOLUBLE STATE; SALT-SOLUTION; SOLUBILITY; WATER;
D O I
10.1016/j.foodres.2016.04.011
中图分类号
TS2 [食品工业];
学科分类号
0832 ;
摘要
Myofibrillar proteins (MPs) of chicken breast are generally insoluble in water. We have developed a new method whereby MPs are solubilized in water by applying high-pressure homogenization (HPH) thus potentially enabling greater utilization of meat in various products. To clarify the mechanism of solubilization of MPs by HPH, we investigated their conformation, solubility and filament forming behavior in low ionic strength solutions induced by 15,000 psi HPH (103 MPa). HPH induces unfolding of MPs which subsequently exposes sulfhydryl and hydrophobic groups to the surface. Our findings, determined by circular dichroism, SDS-PAGE and LC-ESI-MS/MS analysis suggest that HPH leads to unraveling of helical structures and to formation of myosin oligomers through disulfide bond. Due to intermolecular electrostatic repulsion and physical barrier of disulfide bonds in the rod induced by HPH, we suggest that the altered myosin conformation in MPs inhibits filament formation, thus contributing to high solubility of MPs in water. (C) 2016 Elsevier Ltd. All rights reserved.
引用
收藏
页码:1 / 9
页数:9
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