Angiotensin I-converting enzyme inhibitory peptides isolated from tofuyo fermented soybean food
Angiotensin I-converting enzyme inhibitory peptides isolated from tofuyo fermented soybean food
复制标题
DOI：
10.1271/bbb.67.1278
复制
发表时间：
2003-06-01
影响因子：
1.6
通讯作者：
Yasuda, M
中科院分区：
文献类型：
--
作者：
Kuba, M;Tanaka, K;Yasuda, M
在豆腐（发酵大豆食品）提取物中观察到血管紧张素I转化酶（ACE）抑制活性，IC 50值为1.77 mg/ml。采用吸附柱层析、凝胶过滤柱层析、反相高效液相色谱等方法从提取物中分离出ACE抑制剂。纯化的物质与2，4，6-三硝基苯磺酸钠盐反应。通过Edman降解测定的这些抑制剂的氨基酸序列为Ile-Phe-Leu（IC 50，44.8 μ m）和Trp-Leu（IC 50，29.9 μ m）。Ile-Phe-Leu序列存在于β-伴大豆球蛋白的α-和β-亚基中，而Trp-Leu序列存在于大豆球蛋白的B-、B1 A-和BX-亚基中。这两种肽都是非竞争性抑制剂。用胃蛋白酶、胰凝乳蛋白酶或胰蛋白酶处理后，Trp-Leu的抑制活性完全保留。即使在这些胃肠道蛋白酶连续消化后，活性仍保持在原始值的29%。
Angiotensin I-converting enzyme (ACE) inhibitory activity was observed in a tofuyo (fermented soybean food) extract with an IC50 value of 1.77 mg/ml. Two, ACE inhibitors were isolated to homogeneity from the extract by adsorption and gel filtration column chromatography, and by reverse-phase high-performance liquid chromatography (HPLC). The purified substances reacted with 2,4,6-trinitrobenzensulfonic acid sodium salt. The amino acid sequences of these inhibitors determined by Edman degradation were Ile-Phe-Leu (IC50, 44.8 mum) and Trp-Leu (IC50, 29.9 mum). The Ile-Phe-Leu sequence is found in the alpha- and beta-subunits of beta-conglycinin, while the Trp-Leu sequence is in the B-, B1A- and BX-subunits of glycinin from soybean. Both of the peptides are non-competitive inhibitors. The inhibitory activity of Trp-Leu was completely preserved after a treatment with pepsin, chymotrypsin or trypsin. Even after successive digestion by these gastrointestinal proteases, the activity remained at 29% of the original value.