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

¹ Research & Development Center, The Calpis Food Industry Co., Ltd., 5-11-10 Fuchinobe, Sagamihara, Kanagawa 229, Japan and Department of Agricultural Chemistry, Faculty of Agriculture, Tokyo University, Bunkyo-ku, Tokyo 113, Japan

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.

Key Words: angiotensin I-converting enzyme • inhibitor • sour milk • purification

Submitted on July 26, 1994
Accepted on December 12, 1994

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