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 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.
Nakamura
Y
Y
Research & Development Center, Calpis Food Industry Co., Ltd., Kanagawa, Japan.
Yamamoto
N
N
Sakai
K
K
Okubo
A
A
Yamazaki
S
S
Takano
T
T
D000595:Amino Acid Sequence; D000806:Angiotensin-Converting Enzyme Inhibitors / Q000302:isolation & purification*; D000818:Animals; D002851:Chromatography, High Pressure Liquid; D005285:Fermentation; D007778:Lactobacillus; D008892:Milk / Q000737:chemistry* / Q000382:microbiology; D008969:Molecular Sequence Data; D012441:Saccharomyces cerevisiae
D000806:Angiotensin-Converting Enzyme Inhibitors