Antifreeze　proteins　(AFPs)　have　thermal　hysteresis　activity　and　recrystallization-inhibiting　activity,　and　have　potential　applications　in　a　wide　range　of　areas　such　as　the　quality　control　of　frozen　foods,　low　temperature　protection　of　bacteria,　and　plant　protection　against　frost　injury.This　paper　focuses　on　the　theoretical　problem　of　how　AFPs,　containing　a　wide　variety　of　components　with　complicated　structures,　can　inhibit　the　growth　of　ice　crystals　and　exert　thermal　hysteresis　and　recrystallization-inhibiting　activity　by　regulating　the　structure　of　the　ice-water　interface　and　interacting　with　or　binding　to　ice　crystals　in　the　cryogenic　freezing　environment.Meanwhile,　this　review　also　systematically　describes　the　principles　and　characteristics　of　some　related　theoretical　models,　including　adsorption-inhibition　model,　dipole-dipole　model,　lattice　matching　and　possession　model,　rigid　body　energy　model,　anchored　clathrate　model,　and　affinity　interaction　coupling　and　aggregation　model,　and　it　reveals　the　mechanism　by　which　AFPs　bind　to　or　interact　with　the　ice-water　system　by　regulating　the　structure　of　the　ice-water　interface　layer　and　its　driving　force　characteristics.This　review　will　provide　theoretical　guides　for　the　elaboration　of　the　antifreeze　mechanism　and　the　screening　for　application　in　the　food　industry　of　AFPs.　©　2021,　China　Food　Publishing　Company.　All　right　reserved.