Nakamura Y, Yamamoto N, Sakai K, Okubo A, Yamazaki S, Takano T
Research & Development Center, Calpis Food Industry Co., Ltd., Kanagawa, Japan.
J Dairy Sci. 1995 Apr;78(4):777-83. doi: 10.3168/jds.S0022-0302(95)76689-9.
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.
在用含有瑞士乳杆菌和酿酒酵母的可尔必思酸奶发酵剂发酵过程中，牛奶中血管紧张素I转换酶的抑制活性增强。通过四步高效液相色谱法从酸奶中纯化出两种抑制血管紧张素I转换酶的肽。这些抑制剂的氨基酸序列被鉴定为缬氨酸-脯氨酸-脯氨酸和异亮氨酸-脯氨酸-脯氨酸。对血管紧张素I转换酶产生50%抑制作用的肽浓度分别为9微摩尔和5微摩尔。酸奶中的大部分抑制活性归因于这两种肽。
