IDENTIFICATION OF ANGIOTENSIN I-CONVERTING ENZYME INHIBITORY PEPTIDES DERIVED FROM THE PEPTIC DIGEST OF SOYBEAN PROTEIN |
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| Authors: | JIUN-RONG CHEN TAKASHI OKADA KOJI MURAMOTO KUNIO SUETSUNA SUH-CHING YANG |
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| Affiliation: | Department of Nutrition and Health Sciences Taipei Medical University Taipei 110, Taiwan;Department of Bioresources Chemistry Faculty of Agriculture Tohoku University Sendai 981–8555, Japan;Department of Food Science and Technology National Fisheries University Yamaguchi 759–6595, Japan |
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| Abstract: | 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 add sequences of which were identified by Edman's procedure as: Ile‐Ata (inhibitory against ACE with an IC50of 153 μM), Tyr‐Leu‐Ala‐Gly‐Asn‐Gln (14 μM), Phe‐Phe‐Leu (37 μM), Ile‐Tyr‐Leu‐Leu (42 μM), and Val‐Met‐Asp‐Lys‐Pro‐Gln‐Gly (39 μM). The antihypertensive activity of the soybean peptides was also investigated. Peptide fractions (2.0 g/kg body weight, oral administration) markedly towered the blood pressure of spontaneously hypertensive rats (SHRs). |
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