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Journal of Zhejiang University SCIENCE B 2005 Vol.6 No.6 P.508~513

10.1631/jzus.2005.B0508


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


Author(s):  HE Guo-qing, XUAN Guo-dong, RUAN Hui, CHEN Qi-he, XU Ying

Affiliation(s):  Department of Food Science and Nutrition, Zhejiang University, Hangzhou 310029, China

Corresponding email(s):   gqhe@zju.edu.cn

Key Words:  Angiotensin I-converting enzyme inhibitor, Rice dregs, Response surface methodology


HE Guo-qing, XUAN Guo-dong, RUAN Hui, CHEN Qi-he, XU Ying. Optimization of angiotensin I-converting enzyme (ACE) inhibition by rice dregs hydrolysates using response surface methodology[J]. Journal of Zhejiang University Science B, 2005, 6(6): 508~513.

@article{title="Optimization of angiotensin I-converting enzyme (ACE) inhibition by rice dregs hydrolysates using response surface methodology",
author="HE Guo-qing, XUAN Guo-dong, RUAN Hui, CHEN Qi-he, XU Ying",
journal="Journal of Zhejiang University Science B",
volume="6",
number="6",
pages="508~513",
year="2005",
publisher="Zhejiang University Press & Springer",
doi="10.1631/jzus.2005.B0508"
}

%0 Journal Article
%T Optimization of angiotensin I-converting enzyme (ACE) inhibition by rice dregs hydrolysates using response surface methodology
%A HE Guo-qing
%A XUAN Guo-dong
%A RUAN Hui
%A CHEN Qi-he
%A XU Ying
%J Journal of Zhejiang University SCIENCE B
%V 6
%N 6
%P 508~513
%@ 1673-1581
%D 2005
%I Zhejiang University Press & Springer
%DOI 10.1631/jzus.2005.B0508

TY - JOUR
T1 - Optimization of angiotensin I-converting enzyme (ACE) inhibition by rice dregs hydrolysates using response surface methodology
A1 - HE Guo-qing
A1 - XUAN Guo-dong
A1 - RUAN Hui
A1 - CHEN Qi-he
A1 - XU Ying
J0 - Journal of Zhejiang University Science B
VL - 6
IS - 6
SP - 508
EP - 513
%@ 1673-1581
Y1 - 2005
PB - Zhejiang University Press & Springer
ER -
DOI - 10.1631/jzus.2005.B0508


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).

Darkslateblue:Affiliate; Royal Blue:Author; Turquoise:Article

Reference

[1] Baek, H.H., Cadwallader, K.R., 1995. Enzymatic hydrolysis of crayfish processing by-products. Journal of Food Science, 60(5):929-935.

[2] Chen, Q.H., He, G.Q., Mokhtar, A.M., 2002. Optimization of medium composition for the production of elastase by Bacillus sp. EL31410 with response surface methodology. Enzyme and Microbial Technology, 30(5):667-672 (in Chinese).

[3] Diniz, F.M., Martin, A.M., 1996. Use of response surface methodology to describe the combined effects of pH, temperature and E/S ratio on the hydrolysis of dogfish (Squalus acanthias) muscle. International Journal of Food and Technology, 31(5):419-426.

[4] Haaland, P.D., 1989. Statistical Problem Solving. In: Experimental Design in Biotechnology. Marcel Dekker, Inc., New York and Basel, p.1-18.

[5] Ibanoglu, S., Ibanoglu, E., Ainsworth, P., 1998. Effect of dilute acid hydrolysis on the cooked viscosity of tarhana, a traditional Turkish cereal soup. International Journal of Food Science and Nutrition, 49(6):463-466.

[6] Khuri, A.I., Cormell, J.A., 1987. Response Surfaces: Designs and Analysis. Marcel Dekker, New York.

[7] Koike, H., Ito, K., Miyamoto, M., Nishino, H., 1980. Effects of long-term blockade of angiotensin-converting enzyme with captopril (SQ 14, 225) on hemodynamics and circulating blood volume in SHR. Hypertension, 2(3):229-303.

[8] Liu, F.F., Ang, C.Y.W., Springer, D., 2000. Opitimization of extraction conditions for active components in Hypericum perforatum using response surface methodology. Journal of Agricultural and Food Chemistry, 48(8):3364-3371.

[9] Maruyama, S., Miyoshi, S., Kaneko, T., Tanaka, H., 1989. Angiotensin I-converting enzyme inhibitory activites of syntheticpeptides related to the tandem repeated sequence of a maize endosperm protein. Agricultural and Biological Chemistry, 51(2):1581-1586.

[10] Montagomery, D.C., 1991. Design and Analysis of Experiments. 3rd Ed., Wiley, NY.

[11] Ondetti, M.A., Rubin, B., Cushman, D.W., 1977. Design of specific inhibitors of angiotensin I-converting enzyme: New class of orally active antihypertensive agents. Science, 196(1):441-444.

[12] Oshima, G., Shimabukuro, H., Nagasawa, K., 1979. Peptide inhibitors of angiotensin I-converting enzyme in digests of gelatin by bacterial collagenase. Biochimica et Biophysica Acta, 566(1):128-137.

[13] Seki, E., Osajima, K., Matsufuji, H., Matsui, T., Osajima, Y., 1995. Val-Tyr, an angiotensin I-converting enzyme inhibitor from sardines that have resistence to gastrointestinal proteases. Nippon Nogeikagaku Kaishi, 69(4):1013-1020.

[14] Vermeissen, V., Van Bent, A., Van Camp, J., Van Amerongen, A., Verstraete, W., 2004. A quantitative in silico analysis calculates the angiotensin I-converting enzyme (ACE) inhibitory activity in pea and whey protein digests. Biochimie, 86(3):231-239.

[15] Yoshii, H., Tachi, N., Sakamura, O., Takeyama, H., Ohba, R., Itani, T., 1999. Antihypertensive effect of oligo-peptide derived from hens eggs. Nippon Shokuhin Kagaku Kogaku Kaishi, 46(12):45-50.

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<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

Please provide your name, email address and a comment





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