Effects of Oxidation and Different Ionic Environment on the Binding of Pork Myofibrillar Protein to Flavor Substances

The changes of structure and function of pork myofibrillar protein induced by oxidation and its ability to bind flavor substances under different ionic conditions were studied. 2-methyl-butanal, 3-methyl-butanal, hexanal, octanal and nonanal were selected as volatile compounds in the experiment. The ability of myofibrillar protein to bind volatile compounds was observed by headspace combined gas chromatography. The results confirmed that the secondary structure and function of oxidized myofibrillar protein changed. Oxidized myofibrillar protein could promote the release of 2-methyl-butanal and nonanal. Moreover, the effect of oxidized myofibrillar protein on 3-methyl-butanal, hexanal and octanal was dependent on AAPH concentration. The addition of Na⁺ promoted the release of hexanal, while the addition of Na⁺, K⁺, Ca²⁺ and Mg²⁺ promoted the absorption of 2-methyl-butanal, 3-methyl-butanal, octanal and nonal. Consequently, during the processing and storage of meat and meat products, oxidation of meat protein could change its structure and function, and then affect the ability of protein to combine flavor substances. In addition, sodium chloride is partially replaced by other salts in meat products, resulting in changes in the ionic environment of proteins, resulting in changes in the ability of proteins to combine flavor substances, thus changing the flavor of meat products.