This　study　aimed　to　isolate　and　characterise　a　novel　sericin　antifreeze　peptide　and　investigate　its　ice-binding　molecular　mechanism.　The　thermal　hysteresis　activity　of　ice-binding　sericin　peptides　(I-SP)　was　measured　and　their　activity　reached　as　high　as　0.94　degrees　C.　A　P4　fraction,　with　high　hypothermia　protective　activity　and　inhibition　activity　of　ice　recrystallisation,　was　obtained　from　1-SP,　and　a　purified　sericin　peptide,　named　SM-AFP,　with　the　sequence　of　TTSPTNVSTT　and　a　molecular　weight　of　1009.50　Da　was　then　isolated　from　the　P4　fraction.　Treatment　of　Lactobacillus　delbrueckii　Subsp.　bulgaricus　LB340　LYO　with　100　mu　g/ml　synthetic　SM-AFP　led　to　1.4-fold　increased　survival　(p　＜　0.05).　Finally,　an　SM-AFP/ice　binding　model　was　constructed　and　results　of　molecular　dynamics　simulation　suggested　that　the　binding　of　SM-AFP　with　ice　and　prevention　of　ice　crystal　growth　could　be　attributed　to　hydrogen　bond　formation,　hydrophobic　interaction　and　non-bond　interactions.　Sericin　peptides　could　be　developed　into　beneficial　cryoprotectants　and　used　in　frozen　food　processing.　(C)　2014　Elsevier　Ltd.　All　rights　reserved.