Optimization of angiotensin I-converting enzyme (ACE) inhibition by rice dregs hydrolysates using response surface methodology.

Optimization of angiotensin I-converting enzyme (ACE) inhibition by rice dregs hydrolysates using response surface methodology. Research Abstract Details 

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Optimization of angiotensin I-converting enzyme (ACE) inhibition by rice dregs hydrolysates using response surface methodology. Abstract Text:

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).

Optimization of angiotensin I-converting enzyme (ACE) inhibition by rice dregs hydrolysates using response surface methodology. Publishing Authors By Initials

For similar proteins: protein hydrolysates research abstracts see: proteins: protein hydrolysates research

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Optimization of angiotensin I-converting enzyme (ACE) inhibition by rice dregs hydrolysates using response surface methodology. Journal Published:

PUBLICATION TYPE: Journal Article

Journal: Journal of Zhejiang University. Science. B

VOLUME: 6

Page Numbers: 508-13

Journal Abbreviation:

ISSN: 1673-1581

DAY: 25

MONTH: Jun

YEAR: 2005

Optimization of angiotensin I-converting enzyme (ACE) inhibition by rice dregs hydrolysates using response surface methodology. Information

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LANGUAGE: eng

NlmUniqueID: 101236535

Optimization of angiotensin I-converting enzyme (ACE) inhibition by rice dregs hydrolysates using response surface methodology. Keywords Mesh Terms:

KEYWORDS: Protein Hydrolysates

MESH TERMS: chemistry

Chemical & Substance for Abstract: Optimization of angiotensin I-converting enzyme (ACE) inhibition by rice dregs hydrolysates using response surface methodology. Information

Substance Name: Peptidyl-Dipeptidase A

Registry Number: EC 3.4.15.1

Grant and Affiliation Information for Optimization of angiotensin I-converting enzyme (ACE) inhibition by rice dregs hydrolysates using response surface methodology.

AFFILIATION: Department of Food Science and Nutrition, Zhejiang University, Hangzhou 310029, China. gqhe@zju.edu.cn

Country: China

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MEDLINETA: J Zhejiang Univ Sci B

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