This　study　aims　to　explore　the　cryoprotective　mechanisms　of　food-derived　hydrolyzed　peptides　and　develop　novel　cryoprotectants　to　enhance　the　quality　of　frozen　foods.　Evynnis　japonica　scale　antifreeze　peptides　(Ej-AFP)　were　prepared　using　enzymatic　hydrolysis,　which　had　a　4-fold　increase　in　protection　efficiency　for　surimi　compared　to　traditional　cryoprotectants.　Furthermore,　Ej-AFP　was　able　to　control　63.60%　of　the　ice　crystals　to　sizes　below　600　mu　m2.　Three　antifreeze　peptide　sequences　were　purified　by　using　ice-affinity　techniques　and　peptidomics.　These　sequences　demonstrated　a　21.75%　enhancement　in　antifreeze　activity　and　an　increase　of　1　degrees　C　in　thermal　hysteresis　activity　compared　to　Ej-AFP.　Molecular　simulation-elucidated　ice-binding　surface　interacts　with　ice　crystals　through　hydrogen　bonds,　while　the　nonice-binding　surface　disrupts　the　orderly　arrangement　of　water　molecules.　This　results　in　a　tightly　structured　hydration　layer　around　the　peptide,　increasing　the　curvature　of　the　ice　crystal　surface　and　thereby　demonstrating　significant　antifreeze　activity　in　controlling　ice　crystal　growth.