1. Academic Validation
  2. Purification and characterization of angiotensin I-converting enzyme inhibitors from sour milk

Purification and characterization of angiotensin I-converting enzyme inhibitors from sour milk

  • J Dairy Sci. 1995 Apr;78(4):777-83. doi: 10.3168/jds.S0022-0302(95)76689-9.
Y Nakamura 1 N Yamamoto K Sakai A Okubo S Yamazaki T Takano
Affiliations

Affiliation

  • 1 Research & Development Center, Calpis Food Industry Co., Ltd., Kanagawa, Japan.
Abstract

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 microM, respectively. Most of the inhibitory activity in sour milk was attributed to these two Peptides.

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