期刊
BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY
卷 67, 期 6, 页码 1278-1283出版社
TAYLOR & FRANCIS LTD
DOI: 10.1271/bbb.67.1278
关键词
angiotensin I-converting enzyme inhibitor; bioactive peptide; fermented soybean food; tofuyo
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.
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