In　order　to　investigate　the　influence　of　antifreeze　peptide　properties　on　its　protective　effect　on　myofibrillar　proteins　in　frozen　surimi,　the　present　study　was　conducted　to　characterize　the　properties　of　three　antifreeze　peptides　(sericin　peptides,　collagen　peptides　and　silver　carp　hydrolysates),　and　we　analyzed　the　changing　pattern　of　myofibrillar　protein　properties　under　different　freezing　conditions,　and　constructed　a　correlation　model　between　myofibrillar　protein　properties　and　frozen　storage　parameters　and　antifreeze　peptide　properties　using　least　absolute　shrinkage　and　selection　operator　(Lasso)　regression.　The　results　showed　that　all　antifreeze　peptides　used　in　the　study　were　＇hyperactive＇　antifreeze　peptides　with　thermal　hysteresis　activity　(THA)　(＞　0.60　℃),　low　molecular　mass　(2+-ATPase　activity　was　1.61–1.67　U/mg,　the　mean　surface　hydrophobicity　index　increased　only　by　39.91%–42.40%　when　compared　with　that　of　fresh　surimi,　and　the　rate　of　myofibrillar　protein　denaturation　was　much　lower　than　that　of　the　control　group　without　antifreeze　peptides.　The　Lasso　regression　model　explained　the　effects　of　antifreeze　peptide　properties　on　changes　in　the　properties　of　myofibrillar　protein　in　frozen　surimi,　demonstrating　that　antifreeze　peptides　with　lower　molecular　mass　and　higher　THA　contributed　to　slowing　down　the　decline　in　myofibrillar　protein　content,　Ca2+-ATPase　activity,　surface　hydrophobicity,　and　characteristic　indexes.　The　differences　in　the　hydrophilicity/hydrophobicity　of　antifreeze　peptides　resulted　in　differences　in　their　interactions　with　ice　crystals　and　proteins,　and　consequently　caused　different　effects　on　surimi　myofibrillar　proteins.　This　study　provides　a　theoretical　basis　for　the　application　of　antifreeze　peptides　and　the　quality　regulation　of　surimi　products　and　also　provides　a　direction　for　the　development　of　novel　efficient　antifreeze　agents.　©　2024　Chinese　Chamber　of　Commerce.　All　rights　reserved.