Cold-induced denaturation of muscle proteins in hairtail (Trichiurus lepturus) during storage: Physicochemical and label-free based proteomics analyses.

ABSTRACT: Physicochemical, proteomics, and bioinformatics analyses were conducted to investigate protein profiles in Trichiurus haumela under frozen (120 d) and chilled (6 d) storage. Springiness, chewiness, myofibrillar active sulfhydryl content, and Ca²⁺-ATPase activity significantly decreased, suggesting that cold stress altered muscle proteins. Compared with fresh hairtail (FH), 66 common differentially abundant proteins (DAPs) had lower abundances in chilled (3 d; CSH) and frozen (120 d; FSH) hairtail, including myosin binding proteins, filamins, actinin, troponin, and muscle-restricted coiled-coil protein. Gene Ontology (GO) annotation showed DAPs were mainly involved in cellular process, cellular anatomical entity, intracellular, and binding items. Eukaryotic orthologous gro

SUBMITTER: Shui S 

PROVIDER: S-EPMC9583035 | biostudies-literature | 2022 Dec

REPOSITORIES: biostudies-literature