Abstract
The in-vitro digestive properties of myofibrillar protein (MP) in mirror carp (Cyprinus carpio L.) after freeze-thaw (F-T) cycles were analyzed in terms of the relationship between protein degradation, oxidation, and structural properties. The F-T samples exhibited a significant increase in glucosidase activity, N-acetyl-β-d-glucosidase activity, total protease activity, and non-protein nitrogen content. α-aminoadipate semialdehyde and γ-glutamate semialdehyde contents increased by 23.17% and 123.12%, respectively. Furthermore, 53.97% decrease in the total nitrogen content and changes in the content of different soluble proteins were observed. X-ray diffraction intensity, thermal stability, free amine content, hydrolysis degree, and digestibility of the MP samples decreased, and the 2θ angle and zeta potential were reversed. Besides, changes in the amide band wavenumbers were also detected. Therefore, the protein structure was unfolded and aggregates were formed through degradation and oxidation induced by the F-T cycles, ultimately making the in-vitro digestion of MP difficult.
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