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.
- 1. Research & Development Center, Calpis Food Industry Co., Ltd., Kanagawa, 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 microM, respectively. Most of the inhibitory activity in sour milk was attributed to these two peptides.
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Cat. No.Product NameDescriptionTargetResearch Area
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target: Angiotensin Receptor
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Research Areas: Cardiovascular Disease
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target: Angiotensin Receptor
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Research Areas: Cardiovascular Disease