PURIFICATION AND CHARACTERIZATION OF ANGIOTENSIN I-CONVERTING ENZYME-INHIBITORS FROM SOUR MILK

被引：736

作者：

NAKAMURA, Y ^{[1
]}

YAMAMOTO, N ^{[1
]}

SAKAI, K ^{[1
]}

OKUBO, A ^{[1
]}

YAMAZAKI, S ^{[1
]}

TAKANO, T ^{[1
]}

机构：

[1] UNIV TOKYO, FAC AGR, DEPT AGR CHEM, BUNKYO KU, TOKYO 113, JAPAN

来源：

JOURNAL OF DAIRY SCIENCE | 1995年 / 78卷 / 04期

关键词：

ANGIOTENSIN I-CONVERTING ENZYME; INHIBITOR; SOUR MILK; PURIFICATION;

D O I：

10.3168/jds.S0022-0302(95)76689-9

中图分类号：

S8 [畜牧、动物医学、狩猎、蚕、蜂];

学科分类号：

0905 ;

摘要：

The inhibitory activity of angiotensin I-converting enzyme in milk increased during fermentation with the Calpis sour milk starter containing Lactobacillus helveticus and Saccharomyces cerevisiae. Two kinds of peptides inhibitory to angiotensin I-converting enzyme were purified from the sour milk by using four-step HPLC. The amino acid sequences of these inhibitors were identified as Val-Pro-Pro and Ile-Pro-Pro. The concentrations of peptides providing 50% inhibition of angiotensin I-converting enzyme were 9 and 5 mu M, respectively. Most of the inhibitory activity in sour milk was attributed to these two peptides.

引用

页码：777 / 783

页数：7

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