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Updated: Aug 22, 2025
Identification of Plant Ice-binding Proteins Through Assessment of Ice-recrystallization Inhibition and Isolation Using Ice-affinity Purification
Published on: May 5, 2017
Screening and characterization of a novel antifreeze peptide from silver carp muscle hydrolysate
Meili Cui1, Jialei Li1, Jun Li1
1Hunan 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.
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.
