Studies on the Binding Interactions of Grass Carp (Ctenopharyngodon idella) Myosin with Chlorogenic Acid and Rosmarinic Acid
Yuan Huang, Hongying Du, Ghulam Mustafa Kamal, Qiongju Cao, Chen Liu, Shanbai Xiong, Anne Manyande, Qilin Huang
Food and Bioprocess Technology
There are many polyphenols used for the preservation of fish, but the interaction mechanism between polyphenols and fish protein is rarely reported. In the present study, the interactions between two kinds of polyphenols (chlorogenic acid (CGA) and rosmarinic acid (RA)) and the myosin of grass carp (Ctenopharyngodon idella) were explored using multi-spectroscopic techniques. Both CGA and RA were found to be involved in reducing the intrinsic fluorescence and surface hydrophobicity of myosin and increasing the UV absorption intensity. This indicates that interactions between CGA, RA, and myosin ultimately result in the formation of polyphenol-myosin complexes. The binding process of CGA and RA for the formation of the complex was spontaneous. The main binding forces between RA and myosin are hydrogen bonding and van der Waals forces, whereas hydrophobic interactions were observed between CGA and myosin. The results of circular dichroism (CD) showed that the presence of CGA and RA increased the content of myosin alpha-helix. CGA and RA caused myosin aggregation which reduced the corresponding solution dispersibility. CGA and RA protected the myosin sulfhydryl groups and reduced the degree of their oxidation. Furthermore, the complexes formed by the combination of myosin, CGA, and RA exhibited the strongest synergistic antioxidant properties than any one of them. The findings of the present study provide insights into our understanding of the mechanism of interactions between myosin and polyphenols which could provide information on the application of polyphenols in preserving aquatic products.
Circular dichroism, Secondary structure, Ligand binding, Biochemistry, Food science