Antifreeze peptides (AFPs) represent an emerging class of antifreeze agents, offering significant advantages over traditional cryoprotectants and natural antifreeze proteins. To develop a high-activity AFPs derived from silver carp parvalbumin (PV),and explore their potential application in the preservation of frozen foods, PV was purified from fish muscle, and high-activity AFP fractions were obtained through controlled enzymatic hydrolysis and ultrafiltration, with the cryoprotective efficacy of the resulting products on yeast serving as the screening index. The generated optimal fraction was further characterized by UPLC-MS/MS analysis. The results showed that PV from silver carp muscle could be purified effectively by heat treatment. The hydrolysate exhibited optimal antifreeze activity under the conditions of a mass concentration of 30g/L PV, 3000U/g trypsin, and a hydrolysis time of 120min. Under this condition, the prepared AFPs increased the survival rate of freeze-thawed yeast cells to over 90%. Ultrafiltration separation yielded a high-activity fraction F1 (molecular weight of less than 1kDa), which had a thermal hysteresis activity of 1.20℃ and significant ice recrystallization inhibition activity. Yeast treated with the F1 fraction exhibited a survival rate of 51% after three freeze-thaw cycles, and concurrently the OD₆₀₀ showed a moderate decline from 20.6 (fresh) to 11.8. In contrast, the untreated control yeast demonstrated significantly lower survival rate (1%) and OD₆₀₀ (0.9). UPLC-MS/MS analysis identified 417 PV-derived peptides in F1, with 86% of them exhibiting molecular weights ranging from 0.5 to 2.0kDa. Seven of the eight most abundant peptides were predicted to be AFPs, aligning with the good antifreeze activity of F1. The research aimed to innovate a method for preparing highly active antifreeze peptides using pure silver carp PV, laying a foundation for further research on the structure-activity relationship of its highly active AFPs.