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 journalArticle

55 Citations (Scopus)

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 languageEnglish
Pages (from-to)543-554
Number of pages12
JournalJournal of Food Biochemistry
Volume26
Issue number6
Publication statusPublished - Dec 2002

Fingerprint

Soybean Proteins
peptidyl-dipeptidase A
Peptidyl-Dipeptidase A
soy protein
Digestion
digestion
peptides
Soybeans
Peptides
soybeans
antihypertensive effect
Blood pressure
Ion Exchange Chromatography
Inbred SHR Rats
ion exchange chromatography
Chromatography
oral administration
Antihypertensive Agents
Inhibitory Concentration 50
blood pressure

ASJC Scopus subject areas

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

Cite this

Identification of angiotensin I-converting enzyme inhibitory peptides derived from the peptic digest of soybean protein. / Chen, Jiun-Rong; Okada, Takashi; Muramoto, Koji; Suetsuna, Kunio; Yang, Suh-Ching.

In: Journal of Food Biochemistry, Vol. 26, No. 6, 12.2002, p. 543-554.

Research output: Contribution to journalArticle

@article{752740c8382d48e4bf524c3c4f3fef68,
title = "Identification of angiotensin I-converting enzyme inhibitory peptides derived from the peptic digest of soybean protein",
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).",
author = "Jiun-Rong Chen and Takashi Okada and Koji Muramoto and Kunio Suetsuna and Suh-Ching Yang",
year = "2002",
month = "12",
language = "English",
volume = "26",
pages = "543--554",
journal = "Journal of Food Biochemistry",
issn = "0145-8884",
publisher = "Wiley/Blackwell (10.1111)",
number = "6",

}

TY - JOUR

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).

UR - http://www.scopus.com/inward/record.url?scp=0037002214&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0037002214&partnerID=8YFLogxK

M3 - Article

AN - SCOPUS:0037002214

VL - 26

SP - 543

EP - 554

JO - Journal of Food Biochemistry

JF - Journal of Food Biochemistry

SN - 0145-8884

IS - 6

ER -