Abstract
The objective of this study was to elucidate the influence of oxidative modifications of myofibrillar proteins (MPs) on their surface properties. Oxidative modifications (deamination, formation of disulfide bonds and Schiff bases), particle size, net surface charge, and binding ability of volatiles (2-enthylfuran, 1-octen-3-ol, hexanal, and octanal) of oxidized MPs was measured. Molecular docking of volatiles with actomyosin was performed using Qvina-W program and the specific oxidative modifications (monoxidation and deamination) of MPs were determined using LC-MS/MS. Results showed that oxidation of Cys (forming sulfinic, sulfonic, sulfenic acid, and disulfide bonds), monoxidation of Ala, Lys, Glu, and Asn, and deamination of Lys changed the surface properties of oxidized MPs including enhanced surface hydrophobicity and decreased affinity to volatile compounds and water. Overall, this study gives evidence of how protein oxidation affects the properties of MPs and therefore deteriorates fish meat quality.
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