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Journal of Zhejiang University SCIENCE B
ISSN 1673-1581(Print), 1862-1783(Online), Monthly
2005 Vol.6 No.6 P.508-513
Optimization of angiotensin I-converting enzyme (ACE) inhibition by rice dregs hydrolysates using response surface methodology
Abstract: Angiotensin I-converting enzyme (ACE) inhibitory peptides have been shown to have antihypertensive effects and have been utilized for physiologically functional foods and pharmaceuticals. The ACE inhibitory ability of a hydrolysate is determined by its peptide composition. However, the peptide composition of a hydrolysate depends on proteolytic enzyme and the hydrolysis conditions. In this study, the effect of process conditions on the ACE inhibitory activity of rice dregs hydrolyzed with a trypsin was investigated systematically using response surface methodology. It was shown that the ACE inhibitory activity of rice dregs hydrolysates could be controlled by regulation of five process conditions. Hydrolysis conditions for optimal ACE inhibition were defined using the response surface model of fractional factorial design (FFD), steepest ascent design, and central composite design (CCD).
Key words: Angiotensin I-converting enzyme inhibitor, Rice dregs, Response surface methodology
References:
Open peer comments: Debate/Discuss/Question/Opinion
<1>
Munkhjargal@Ass. prof in department of School of Chemistry and chemical engineering National university of Mongolia<monkhjargal@num.edu.mn>
2013-04-27 08:19:01
I am creating assay for ACE inhibitory of bioactive peptides from animal resaurces in our lab. So I am collecting information for this assay methods
DOI:
10.1631/jzus.2005.B0508
CLC number:
TS201.1
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