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Effect of pretreatment on enzymatic hydrolysis of bovine collagen and formation of ACE-inhibitory peptides

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Authors:
  • Zhang, Yuhao ;
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    Food Chemistry, Department of Food Science, Faculty of Life Sciences, Københavns Universitet
  • Olsen, Karsten ;
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    Orcid logo0000-0002-0104-6292
    Food Chemistry, Department of Food Science, Faculty of Science, Københavns Universitet
  • Grossi, Alberto Blak ;
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    Food Chemistry, Department of Food Science, Faculty of Science, Københavns Universitet
  • Otte, Jeanette Anita Held
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    Orcid logo0000-0002-9444-9102
    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

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