Proteolysis of tilapia skin collagen: Identification and release behavior of ACE-inhibitory peptides

The structure-activity relationship (SAR) and release behavior of angiotensin I-converting enzyme inhibitory (ACEi) peptides obtained from enzymolysis of collagen influence the large-scale production of ACEi peptides. However, researchers have paid insufficient attention to these areas. In this study, we extracted collagen from tilapia skin, and hydrolyzed it using three proteases. A total of 270 peptides were released from the collagen parent protein. The SAR of these larger collagen ACEi peptides indicated that the presence of proline at position C2 of three C-terminal sequences has a greater effect on increasing the ACEi activity of the peptide than at position C1. The release behavior of these collagen peptides showed that bromelain and alcalase preferentially cleave the N-terminal region of the collagen alpha(1) subunit and then the C-terminal region. These enzymes evenly cleave regions of the collagen alpha(2) subunit. Collagenase preferentially cleaves the C-terminal region of the collagen subunit, followed by the N-terminal region, and then the middle region. The pattern of peptide release from different proteases and the SAR of larger collagen peptides can help guide food production processes to ensure food safety, and to produce high-quality active peptide products.

Automated summary

The SAR and release behavior of ACEi peptides from collagen enzymolysis have an impact on large-scale production. Different proteases have varied effects on the release of peptides from collagen and the SAR of larger collagen peptides, which can guide food production processes for ensuring food safety and producing high-quality active peptide products.