Effect of pretreatment on enzymatic hydrolysis of bovine collagen and formation of ACE-inhibitory peptides
- Authors:
-
- Zhang, Yuhao ;
-
Olsen, Karsten
;
Close
0000-0002-0104-6292
Food Chemistry, Department of Food Science, Faculty of Science, Københavns Universitet - Grossi, Alberto Blak ;
-
Otte, Jeanette Anita Held
Close0000-0002-9444-9102
Food Chemistry, Department of Food Science, Faculty of Science, Københavns Universitet
- DOI:
- 10.1016/j.foodchem.2013.05.058
- Abstract:
- 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 ACEinhibitory peptides. The highest ACE-inhibitory activity was obtained with Alcalase. Pretreatment significantly influenced the DH and ACE-inhibition. For most enzymes, boiling for 5 min 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.
- Type:
- Journal article
- Language:
- English
- Published in:
- Food Chemistry, 2013, Vol 141, Issue 3, p. 2343-2354
- Main Research Area:
- Science/technology
- Publication Status:
- Published
- Review type:
- Peer Review
- Submission year:
- 2013
- Scientific Level:
- Scientific
- ID:
- 243640052
