Characterization and the mechanism underlying the cryoprotective activity of a peptide from large yellow croaker (Pseudosciaena crocea)

Food Chem. 2024 Mar 1:435:137512. doi: 10.1016/j.foodchem.2023.137512. Epub 2023 Sep 26.

Abstract

Ice crystal-induced protein denaturation is the main cause of the deterioration of fish during frozen storage and transportation. In this study, the ultra-performance liquid chromatography - quadrupole - time of flight (UPLC-Q-TOF) technique was used to identify and screen tryptic peptides Ile-Glu-Glu-Leu-Glu-Glu-Leu-Glu-Ala-Glu-Arg (IEELEEELEAER) from large yellow croaker (Pseudosciaena crocea). The results were used study their cryoprotective effects on turbot fish meat during freeze-thaw cycles at different concentrations, and to investigate their anti-freezing mechanism. The results showed that the I-2.0 group effectively inhibiting the degeneration and structure changes of myofibrillar proteins after three freeze-thaw cycles, and the Ca2+-ATPase activity (1.65 μmolPi/mg/h), increased by 55.86% compared with that of the control group. Additionally, peptide IEELEEELEAER could provide antifreeze protection by binding to the surface of ice crystals and inhibiting their transformation. This peptide acts as a natural cryoprotectant and might be used for the cryogenic storage and transportation of fish products.

Keywords: Antifreeze mechanism; Antifreeze peptide; Enzymatic hydrolysis; Freeze–thaw cycle; Protein oxidation.

MeSH terms

  • Animals
  • Cryoprotective Agents / pharmacology
  • Ice*
  • Peptides / pharmacology
  • Perciformes*
  • Proteins

Substances

  • Ice
  • Peptides
  • Proteins
  • Cryoprotective Agents