Abstract: 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.

Key words: antifreeze protein; antifreeze mechanism; ice-water interface layer; theoretical model