title: Effect of pretreatment on enzymatic hydrolysis of bovine collagen and formation of ACE-inhibitory peptides.
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 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 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.
authors.affiliation: College of Food Science, Southwest University, No. 2 Tiansheng Road, Beibei District, Chongqing 400716, PR China.
authors.forename: Yuhao
authors.initials: Y
authors.lastname: Zhang
authors.forename: Karsten
authors.initials: K
authors.lastname: Olsen
authors.forename: Alberto
authors.initials: A
authors.lastname: Grossi
authors.forename: Jeanette
authors.initials: J
authors.lastname: Otte
mesh_terms: D000806:Angiotensin-Converting Enzyme Inhibitors / Q000737:chemistry* / Q000302:isolation & purification; D000818:Animals; D001709:Biotechnology / Q000379:methods*; D002417:Cattle; D003094:Collagen / Q000737:chemistry*; D006868:Hydrolysis; D006874:Hydrostatic Pressure; D010447:Peptide Hydrolases / Q000737:chemistry*; D010455:Peptides / Q000737:chemistry* / Q000302:isolation & purification; D011492:Protein Hydrolysates / Q000737:chemistry / Q000302:isolation & purification
chemical_list: D000806:Angiotensin-Converting Enzyme Inhibitors; D010455:Peptides; D011492:Protein Hydrolysates; D003094:Collagen; D010447:Peptide Hydrolases
keywords: ACE-inhibition; Boiling; Collagen; DH; Enzymatic hydrolysis; High pressure