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

Jiun-Rong Chen; Takashi Okada; Koji Muramoto; Kunio Suetsuna; Suh-Ching Yang

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

Jiun-Rong Chen, Takashi Okada, Koji Muramoto, Kunio Suetsuna, Suh-Ching Yang

Research output: Contribution to journal › Article › peer-review

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 acid sequences of which were identified by Edman's procedure as: Ile-Ala (inhibitory against ACE with an IC₅₀ of 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 lowered the blood pressure of spontaneously hypertensive rats (SHRs).

Original language	English
Pages (from-to)	543-554
Number of pages	12
Journal	Journal of Food Biochemistry
Volume	26
Issue number	6
Publication status	Published - Dec 2002

ASJC Scopus subject areas

Food Science
Biochemistry, Genetics and Molecular Biology(all)
Biochemistry

Cite this

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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 acid sequences of which were identified by Edman's procedure as: Ile-Ala (inhibitory against ACE with an IC50 of 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 lowered the blood pressure of spontaneously hypertensive rats (SHRs).",

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T1 - Identification of angiotensin I-converting enzyme inhibitory peptides derived from the peptic digest of soybean protein

AU - Chen, Jiun-Rong

AU - Okada, Takashi

AU - Muramoto, Koji

AU - Suetsuna, Kunio

AU - Yang, Suh-Ching

PY - 2002/12

Y1 - 2002/12

N2 - 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 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 lowered the blood pressure of spontaneously hypertensive rats (SHRs).

AB - 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 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 lowered the blood pressure of spontaneously hypertensive rats (SHRs).

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

Abstract

ASJC Scopus subject areas

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