Screening and characterization of a novel antifreeze peptide from silver carp muscle hydrolysate. (1st March 2023)

• Record Type: Journal Article
• Authors: Cui, Meili; Li, Jialei; Li, Jun; Wang, Faxiang; Li, Xianghong; Yu, Jian; Huang, Yiqun; Liu, Yongle
• Is Part Of: Food chemistry. Volume 403(2023)
• Publication Date: 2023-03-01
• Subjects: Fish -- Parvalbumin -- Yeast -- Molecular dynamics -- Homology modeling -- Thermal hysteresis; Food -- Analysis -- Periodicals; Food -- Composition -- Periodicals; 664
• DOI: 10.1016/j.foodchem.2022.134480
• Languages: English
• ISSNs: 0308-8146

Abstract

Highlights: A novel antifreeze peptide (AFP) was obtained from silver carp muscle hydrolysate. The novel AFP (Sc-AFP) was derived from the parvalbumin. Sc-AFP could bind to 48 water molecules and ice surface via hydrogen bonds. An FNHK loop of Sc-AFP was a specific binding site for inhibiting ice growth. 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.