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Effect of pretreatment on enzymatic hydrolysis of bovine collagen and formation of ACE-inhibitory peptides
- Zhang, Yuhao, Olsen, Karsten, Grossi, Alberto, Otte, Jeanette
- Food chemistry 2013 v.141 no.3 pp. 2343-2354
- cattle, collagen, enzymatic hydrolysis, enzymatic treatment, foods, hydrolysates, hydrolysis, peptides, peptidyl-dipeptidase A, pretreatment, subtilisin
- Bovine collagen was pre-treated (boiled or high pressure (HP)-treated) and then hydrolysed by 6 proteases. The degree of hydrolysis (DH) and the angiotensin-converting enzyme (ACE)-inhibitory activity of hydrolysates were measured. All enzymes used were able to partly degrade collagen and release ACE-inhibitory peptides. The highest ACE-inhibitory activity was obtained with Alcalase. Pretreatment significantly influenced the DH and ACE-inhibition. For most enzymes, boiling for 5min resulted in a significantly higher DH and ACE-inhibitory activity. With Alcalase and collagenase, hydrolysis and release of ACE-inhibitory peptides occurred without any pretreatment, but HP-treatment significantly improved the DH and ACE-inhibitory activity. HP did not markedly affect the hydrolysis with the other enzymes. The major peptides obtained with Alcalase were identified; all were released from the triple helix structure of collagen. Many of these peptides had C-terminal sequences similar to known ACE-inhibitory peptides. The present results suggest that collagen-rich food materials are good substrates for the release of potent ACE-inhibitory peptides, when proper pre-treatment and enzymatic treatment is applied.