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CLC number: S872

On-line Access: 2014-01-28

Received: 2013-09-04

Revision Accepted: 2013-12-01

Crosschecked: 2014-01-21

Cited: 6

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Citations:  Bibtex RefMan EndNote GB/T7714

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Journal of Zhejiang University SCIENCE B 2014 Vol.15 No.2 P.143-152


Stability and cytotoxicity of angiotensin-I-converting enzyme inhibitory peptides derived from bovine casein*

Author(s):  Wei Wu, Pan-pan Yu, Feng-yang Zhang, Hong-xia Che, Zhan-mei Jiang

Affiliation(s):  . Key Laboratory of Dairy Science, Ministry of Education, College of Food Science, Northeast Agricultural University, Harbin 150030, China

Corresponding email(s):   zhanmei.jiang@gmail.com

Key Words:  Angiotensin-I-converting enzyme inhibitory peptide, Heat treatment, Stability, Cytotoxicity

Wei Wu, Pan-pan Yu, Feng-yang Zhang, Hong-xia Che, Zhan-mei Jiang. Stability and cytotoxicity of angiotensin-I-converting enzyme inhibitory peptides derived from bovine casein[J]. Journal of Zhejiang University Science B, 2014, 15(2): 143-152.

@article{title="Stability and cytotoxicity of angiotensin-I-converting enzyme inhibitory peptides derived from bovine casein",
author="Wei Wu, Pan-pan Yu, Feng-yang Zhang, Hong-xia Che, Zhan-mei Jiang",
journal="Journal of Zhejiang University Science B",
publisher="Zhejiang University Press & Springer",

%0 Journal Article
%T Stability and cytotoxicity of angiotensin-I-converting enzyme inhibitory peptides derived from bovine casein
%A Wei Wu
%A Pan-pan Yu
%A Feng-yang Zhang
%A Hong-xia Che
%A Zhan-mei Jiang
%J Journal of Zhejiang University SCIENCE B
%V 15
%N 2
%P 143-152
%@ 1673-1581
%D 2014
%I Zhejiang University Press & Springer
%DOI 10.1631/jzus.B1300239

T1 - Stability and cytotoxicity of angiotensin-I-converting enzyme inhibitory peptides derived from bovine casein
A1 - Wei Wu
A1 - Pan-pan Yu
A1 - Feng-yang Zhang
A1 - Hong-xia Che
A1 - Zhan-mei Jiang
J0 - Journal of Zhejiang University Science B
VL - 15
IS - 2
SP - 143
EP - 152
%@ 1673-1581
Y1 - 2014
PB - Zhejiang University Press & Springer
ER -
DOI - 10.1631/jzus.B1300239

This study investigated the effect of heat treatment combined with acid and alkali on the angiotensin-I-converting enzyme (ACE) inhibitory activity of peptides derived from bovine casein. The free amino group content, color, and cytotoxicity of the peptides were measured under different conditions. When heated at 100 °C in the pH range from 9.0 to 12.0, ACE inhibitory activity was reduced and the appearance of the peptides was significantly darkened. After thermal treatment in the presence of acid and alkali, the free amino group content of ACE inhibitory peptides decreased markedly. High temperature and prolonged heating also resulted in the loss of ACE inhibitory activity, the loss of free amino groups, and the darker coloration of bovine casein-derived peptides. However, ACE inhibitory peptides, within a concentration range of from 0.01 to 0.2 mg/ml, showed no cytotoxicity to Caco-2 and ECV-304 cell lines after heat treatment. This indicated that high temperature and alkaline heat treatment impaired the stability of bovine casein-derived ACE inhibitory peptides.


创新要点:在pH 9.0~12.0的热处理条件下,牛乳酪蛋白源ACE抑制肽的抑制活性降低,色泽加深。热处理后的ACE抑制肽对Caco-2细胞和ECV-304细胞没有毒性作用。


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


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