Purification and Characterization of Angiotensin I-Converting Enzyme Inhibitors from Sour Milk

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...

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Bibliographic Details
Published inJournal of dairy science Vol. 78; no. 4; pp. 777 - 783
Main Authors Nakamura, Yasunori, Yamamoto, Naoyuki, Sakai, Kumi, Okubo, Akira, Yamazaki, Sunao, Takano, Toshiaki
Format Journal Article
LanguageEnglish
Published Savoy, IL Elsevier Inc 01.04.1995
Am Dairy Sci Assoc
American Dairy Science Association
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Summary: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 μM, respectively. Most of the inhibitory activity in sour milk was attributed to these two peptides.
Bibliography:9546888
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ISSN:0022-0302
1525-3198
DOI:10.3168/jds.S0022-0302(95)76689-9