Effect of Different Addition Amounts of Capsaicin on the Structure, Oxidation Sites, and Gel Properties of Myofibrillar Proteins under Oxidative Conditions

This study aimed to explore the mechanism influencing different addition amounts of capsaicin on the gel characteristics and microstructure of myofibrillar protein (MP) gels under conditions induced by hydroxyl free radicals (center dot OH). Results indicate that adding capsaicin can improve the gelling characteristics of the MPs. With an increased amount of capsaicin added, the oxidation of MPs by center dot OH decreased, and the number of oxidation sites decreased. Peptides located around residues 651-851 in the head domain SH1 and S2 subunits of the myosin heavy chain were susceptible to oxidation. Capsaicin primarily interacted with amino acids in SH1 (residues 1-151 and 601-651), reducing the effect of center dot OH on MPs and consequently decreasing the occurrence of MP aggregation. Capsaicin protected the structure and oxidation sites of MPs under oxidative conditions, ensuring the formation of an MP gel with uniformly dense pores during heating, thereby improving the texture characteristics and water-holding capacity of the gel.