Identification and characterization of phosphoproteins in the striated and smooth adductor muscles of Yesso scallop Patinopecten yessoensis

Food Chem. 2022 Mar 15:372:131242. doi: 10.1016/j.foodchem.2021.131242. Epub 2021 Sep 30.

Abstract

Many proteins are known to be phosphorylated, affecting important regulatory factors of muscle quality in the aquatic animals. The striated and smooth adductor muscles of Yesso scallop Patinopecten yessoensis were used to investigate muscle texture and identify phosphoproteins by histological methods and phosphoproteomic analysis. Our present study reveals that muscle fiber density is in relation to meat texture of the striated and smooth adductor muscles. The phosphoproteomic analysis has identified 764 down-regulated and 569 up-regulated phosphosites on 743 phosphoproteins in the smooth muscle compared to the striated part. The identification of unique phosphorylation sites in glycolytic enzymes may increase the activity of glycolytic enzymes and the rate of glycolysis in the striated adductor muscle. The present findings will provide new evidences on the role of muscle structure and protein phosphorylation in scallop muscle quality and thus help to develop strategies for improving meat quality of scallop products.

Keywords: Glycolytic enzymes; Meat quality; Myofibrillar proteins; Protein phosphorylation; Scallop.

MeSH terms

  • Animals
  • Muscle, Skeletal
  • Muscle, Smooth
  • Pectinidae*
  • Phosphoproteins* / genetics
  • Seafood

Substances

  • Phosphoproteins