Identification of angiotensin I-converting enzyme inhibitory peptides derived from the peptic digest of soybean protein

被引：44

作者：

Chen, JR

Okada, T

Muramoto, K

Suetsuna, K

Yang, SC ^{[1
]}

机构：

[1] Taipei Med Univ, Dept Nutr & Hlth Sci, Taipei 110, Taiwan

[2] Tohoku Univ, Fac Agr, Dept Bioresources Chem, Sendai, Miyagi 981, Japan

[3] Natl Fisheries Univ, Dept Food Sci & Technol, Yamaguchi 7596595, Japan

来源：

JOURNAL OF FOOD BIOCHEMISTRY | 2002年 / 26卷 / 06期

关键词：

D O I：

10.1111/j.1745-4514.2002.tb00772.x

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Peptidic fractions which inhibit angiotensin I-converting enzyme (ACE) were separated from peptic digests of soybean by ion exchange chromatography and gel filtration. Further separation of the peptidic fractions by ODS HPLC afforded active peptides, the amino acid sequences of which were identified by Edman's procedure as: Ile-Ala (inhibitory against ACE with an IC50 of 153 muM), Tyr-Leu-Ala-Gly-Asn-Gln (14 muM), Phe-Phe-Leu (37 muM), Ile-Tyr-Leu-Leu (42 muM), and Val-Met-Asp-Lys-Pro-Gln-Gly (39 muM). The antihypertensive activity of the soybean peptides was also investigated. Peptide fractions (2.0 g/kg body weight, oral administration) markedly lowered the blood pressure of spontaneously hypertensive rats (SHRs).

引用

页码：543 / 554

页数：12

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