Identification and release kinetics of peptides from tilapia skin collagen during alcalase hydrolysis.

Collagen from tilapia skin was extracted and confirmed as type I collagen. Collagen was then hydrolyzed with alcalase for 4 h and the released peptides were identified. The structure-activity relationship of collagen-released peptides showed that proline at position C3 played a key role in improving ACE inhibitory activity, while proline at position C2 had a negative effect. Collagen peptide release kinetics showed that with the extension of time, the number of peptides increased dramatically at first, decreased, and then tended to be stable. This indicated that collagen peptides mainly originated from primary enzymolysis at the first stage and began to undergo secondary hydrolysis in the second stage. Afterwards, secondary enzymolysis was dominant at the third stage and finally remained stable at final two stages. Understanding the pattern of collagen peptide release kinetics might offer a powerful approach in the collagen-peptide food processing industry to better control food safety and quality.