Protein hydrolysate from tilapia frame: antioxidant and angiotensin I converting enzyme inhibitor properties. (9th March 2015)

• Record Type: Journal Article
• Authors: Chuesiang, Piyanan; Sanguandeekul, Romanee
• Is Part Of: International journal of food science & technology. Volume 50:Number 6(2015:Jun.)
• Page Start: 1436
• Page End: 1444
• Publication Date: 2015-03-09
• Subjects: Food industry and trade -- Periodicals; 664
• DOI: 10.1111/ijfs.12762
• Languages: English
• ISSNs: 0950-5423

Abstract

<abstract abstract-type="main" id="ijfs12762-abs-0001"> <title>Summary</title> <p>The effect of varying the aminopeptidase concentration and hydrolysis time in the production of a protein hydrolysate from tilapia frame (TFPH) was evaluated in terms of the obtained antioxidant and angiotensin I converting enzyme (ACE) inhibitor activities. Minced tilapia frame was subjected to hydrolysis using three concentrations Flavourzyme^® 1000 L [Brenntag Ingredients (Thailand) Company Limited (Public), Bangkok, Thailand] [0%, 1% and 2% (w/w)] and two hydrolysis times (0 and 1 h). The enzyme concentration and hydrolysis time both significantly affected the antioxidant and ACE inhibitor properties. The use of 2% (w/w) Flavourzyme^® 1000 L for 1 h yielded the highest levels of 2, 2‐diphenyl‐1‐picrylhydrazil free radical scavenging (90.4%), metal chelating (91.8%), thiobarbituric acid activity ratio (81.9%), and ACE inhibition (83.8%). In addition, this TFPH contained a higher net amount of amino acids and a larger peptide molecular weight distribution compared to the unhydrolysed tilapia frame supernatant. Thus, TFPH may be a suitable supplement to improve the functionality of food products.</p> </abstract>