Comprehensive binding analysis of glycated myosin with furan derivatives via glucose by means of multi-spectroscopy techniques and molecular docking simulation

Abstract

Myosin is an ideal binding receptor for aroma compounds and its functional properties are easily affected by glucose. The study comprehensively clarified the effects of glucose glycation-induced structural modifications of myosin on its binding ability with furan derivatives, including 2-methylfuran, 2-furfural, and 2-furfurylthiol. The results demonstrated that the binding levels of furan derivatives were obviously affected by the glycation levels of myosin due to the changes of myosin structure and surface. The increased glycation levels caused the unfolding of myosin structure and accelerated the aggregation, as were exhibited by the data of zeta potential, particle size, microstructure, and secondary structure. The glycated myosin with wrinkled surfaces favored the significant increase of hydrophobic interactions (31.59–69.50 μg), the more exposure of amino acid residues (3459–6048), the formation of free sulfhydryl groups (16.37–20.58 mmol/104g) and hydrogen bonds. These key (non)covalent linkages accounted for the generation of glycated myosin-odorants complex, including 2-furfurylthiol (29.17–47.87 %), thus enhancing the resultant binding ability as evidenced by the free furan derivatives concentrations, fluorescence quenching and molecular docking simulation analysis. The glycated myosin for 8 h bound highest concentrations of furan derivatives. The results will provide comprehensive data on the retention of aroma compounds in meat products.