Journal
FOOD SCIENCE AND BIOTECHNOLOGY
Volume 22, Issue 6, Pages 1531-1537Publisher
KOREAN SOCIETY FOOD SCIENCE & TECHNOLOGY-KOSFOST
DOI: 10.1007/s10068-013-0248-9
Keywords
ACE-inhibitory activity; degree of hydrolysis; response surface methodology; optimization; vital wheat gluten
Categories
Funding
- National Natural Science Foundation of China [31071502]
- Priority Academic Program Development (PAPD) of Jiangsu Higher Education Institutions
- National Public Welfare Fields (agriculture) Technology Program of China [201303071]
- Jiangsu provincial science and technology support program of China (Agriculture Section) [BE2013408]
Ask authors/readers for more resources
The degree of hydrolysis (DH) and angiotensin I-converting enzyme (ACE)-inhibitory activity of vital wheat gluten (VWG) hydrolyzed using Alcalase were investigated using Box-Behnken response surface methodology (RSM). The mean responses were fitted to a second order polynomial to obtain regression equations. The enzyme-substrate ratio and the hydrolysis time increased the DH significantly (p<0.05). The substrate.concentration was the only significant linear term leading to an increase in ACE-inhibitory activity. The optimized conditions of a substrate concentration of 5.04%, an enzyme-substrate ratio 5.94%, and a hydrolysis time 30.79 min gave a point prediction of a 12.74% DH and 82.28% ACE-inhibitory activity. Analytical results from confirmatory experiment were a 12.22%+/-0.5 DH and a 78.93%+/-1.07 ACEinhibitory activity. The optimized conditions of the study provide useful information to the functional food and beverage industries to enhance the anti-hypertensive activities of peptides from VWG.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available