Elucidating the molecular mechanism of water migration in myosin gels of Nemipterus virgatus during low pressure coupled with heat treatment

Abstract

The relationship between myosin denaturation, aggregation and water migration in Nemipterus virgatus myosin gels with different treatment processes under optimal low pressure coupled with heat treatment was investigated to clarify the molecular mechanism of water migration. With the different treatment processes, the proportion of bound water of the myosin gels increased significantly (P < 0.05). Denaturation of myosin S1 sub-fragments and α-helical unfolding during different treatment processes led to an increase in β-sheets content. These promote increased exposure of Try residues and hydrophobic groups of myosin, formation of clathrate hydrates, and reduced mobility of bound water. Furthermore, hydrophobic interactions and disulfide bonds caused the head-head and head-hinge to coalesce into a 3D honeycomb network with greater fractal dimension, less lacunarity, smaller water hole diameter and more water holes. This increased the capillary pressure experienced by the bound water, causing immobile water to migrate towards the bound water. The present study may be necessary to improve the mechanism of water migration in protein gel systems and to promote the industrial application of high pressure processing technology in surimi-based foods.