Screening and characterization of a novel antifreeze peptide from silver carp muscle hydrolysate

Meili Cui; Jialei Li; Jun Li; Faxiang Wang; Xianghong Li; Jian Yu; Yiqun Huang; Yongle Liu

doi:10.1016/j.foodchem.2022.134480

Screening and characterization of a novel antifreeze peptide from silver carp muscle hydrolysate

Food Chem. 2023 Mar 1:403:134480. doi: 10.1016/j.foodchem.2022.134480. Epub 2022 Oct 1.

Authors

Meili Cui¹, Jialei Li¹, Jun Li¹, Faxiang Wang², Xianghong Li¹, Jian Yu¹, Yiqun Huang¹, Yongle Liu³

Affiliations

¹ Hunan Provincial Engineering Technology Research Center of Aquatic Food Resources Processing, School of Food Science and Bioengineering, Changsha University of Science and Technology, Changsha 410114, China.
² Hunan Provincial Engineering Technology Research Center of Aquatic Food Resources Processing, School of Food Science and Bioengineering, Changsha University of Science and Technology, Changsha 410114, China. Electronic address: wfx@csust.edu.cn.
³ Hunan Provincial Engineering Technology Research Center of Aquatic Food Resources Processing, School of Food Science and Bioengineering, Changsha University of Science and Technology, Changsha 410114, China. Electronic address: yongleliu@csust.edu.cn.

PMID: 36358085
DOI: 10.1016/j.foodchem.2022.134480

Abstract

This study aimed to screen and characterize antifreeze peptides from silver carp muscle hydrolysate (SCMH). The SCMH was initially fractionated by ultrafiltration, and the resultant SCMH-IV (<10 kDa) showing 90 % of yeast survival rate was subsequently separated into four fractions using ion-exchange chromatography. The fraction with the best antifreeze activity was further analyzed by liquid chromatography-tandem mass spectrometry. A total of 514 peptides were identified, of which a novel antifreeze peptide (Sc-AFP, KAADSFNHKAFFAKVG) with a thermal hysteresis activity of 0.87 ℃ was selected. The parvalbumin-derived Sc-AFP showed an alanine-rich, α-helical and amphipathic character. Based on molecular dynamics simulations, the Sc-AFP could interact with 48 water molecules via hydrogen bonds, and could be adsorbed onto the ice surface through a total of 21 hydrogen bonds mainly linked to the lysine residues. This could account for its antifreeze properties via preventing the formation and growth of ice crystals.

Keywords: Fish; Homology modeling; Molecular dynamics; Parvalbumin; Thermal hysteresis; Yeast.

MeSH terms

Animals
Antifreeze Proteins / chemistry
Carps*
Ice*
Muscles
alpha-Fetoproteins

Substances

Ice
alpha-Fetoproteins
Antifreeze Proteins