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

Xing Chen; Xinglian Xu; Minyi Han; Guanghong Zhou; Conggui Chen; Peijun Li

doi:10.1016/j.foodres.2016.04.011

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

Food Res Int. 2016 Jul:85:1-9. doi: 10.1016/j.foodres.2016.04.011. Epub 2016 Apr 16.

Authors

Xing Chen¹, Xinglian Xu², Minyi Han³, Guanghong Zhou⁴, Conggui Chen⁵, Peijun Li⁶

Affiliations

¹ Key Laboratory of Animal Products Processing, Ministry of Agriculture, Key Laboratory of Meat Processing and Quality Control, Ministry of Education, Jiangsu Synergetic Innovation Center of Meat Production and Processing, and College of Food Science and Technology, Nanjing Agricultural University, Nanjing, Jiangsu 210095, People's Republic of China. Electronic address: cxniigata@163.com.
² Key Laboratory of Animal Products Processing, Ministry of Agriculture, Key Laboratory of Meat Processing and Quality Control, Ministry of Education, Jiangsu Synergetic Innovation Center of Meat Production and Processing, and College of Food Science and Technology, Nanjing Agricultural University, Nanjing, Jiangsu 210095, People's Republic of China. Electronic address: xlxus@njau.edu.cn.
³ Key Laboratory of Animal Products Processing, Ministry of Agriculture, Key Laboratory of Meat Processing and Quality Control, Ministry of Education, Jiangsu Synergetic Innovation Center of Meat Production and Processing, and College of Food Science and Technology, Nanjing Agricultural University, Nanjing, Jiangsu 210095, People's Republic of China. Electronic address: redleafnew@163.com.
⁴ Key Laboratory of Animal Products Processing, Ministry of Agriculture, Key Laboratory of Meat Processing and Quality Control, Ministry of Education, Jiangsu Synergetic Innovation Center of Meat Production and Processing, and College of Food Science and Technology, Nanjing Agricultural University, Nanjing, Jiangsu 210095, People's Republic of China. Electronic address: ghzhou@njau.edu.cn.
⁵ School of Biology and Food Engineering, Hefei University of Technology, Hefei, Anhui 230009, People's Republic of China. Electronic address: chen_conggui@hotmail.com.
⁶ School of Biology and Food Engineering, Hefei University of Technology, Hefei, Anhui 230009, People's Republic of China. Electronic address: li_pj@hotmail.com.

PMID: 29544823
DOI: 10.1016/j.foodres.2016.04.011

Abstract

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 15,000psi HPH (103MPa). HPH induces unfolding of MPs which subsequently exposes sulfhydryl and hydrophobic groups to the surface. Our findings, determined by circular dichroism, ATR-FTIR, 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.

Keywords: Conformation; Filament formation; High-pressure homogenization; Myofibrillar proteins; Myosin; Solubility.