title: Purification and characterization of angiotensin I-converting enzyme inhibitors from sour milk.
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.
authors.affiliation: Research & Development Center, Calpis Food Industry Co., Ltd., Kanagawa, Japan.
authors.forename: Y
authors.initials: Y
authors.lastname: Nakamura
authors.forename: N
authors.initials: N
authors.lastname: Yamamoto
authors.forename: K
authors.initials: K
authors.lastname: Sakai
authors.forename: A
authors.initials: A
authors.lastname: Okubo
authors.forename: S
authors.initials: S
authors.lastname: Yamazaki
authors.forename: T
authors.initials: T
authors.lastname: Takano
mesh_terms: 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
chemical_list: D000806:Angiotensin-Converting Enzyme Inhibitors