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...
Saved in:
Published in | Journal of dairy science Vol. 78; no. 4; pp. 777 - 783 |
---|---|
Main Authors | , , , , , |
Format | Journal Article |
Language | English |
Published |
Savoy, IL
Elsevier Inc
01.04.1995
Am Dairy Sci Assoc American Dairy Science Association |
Subjects | |
Online Access | Get full text |
Cover
Loading…
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 S30 Q02 ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 23 ObjectType-Article-1 ObjectType-Feature-2 |
ISSN: | 0022-0302 1525-3198 |
DOI: | 10.3168/jds.S0022-0302(95)76689-9 |