Preparation and characterization of novel bioactive peptides responsible far angiotensin I-converting enzyme inhibition from wheat germ

Toshiro Matsui, Chun Hui Li, Yutaka Osajima

Research output: Contribution to journalArticle

132 Citations (Scopus)

Abstract

Reported is the preparation of wheat germ (WG) hydrolyzate with potent angiotensin I-converting enzyme (ACE) inhibitory activity, and the characterization of peptides responsible for ACE inhibition. Successful hydrolyzate with the most potent ACE inhibitory activity was obtained by 0.5 wt. %-8 h Bacillus licheniformis alkaline protease hydrolysis after 3.0 wt. %-3 h α-amylase treatment of defatted WG (IC50; 0.37 mg protein ml-1). The activity of WG hydrolyzate was markedly increased by ODS and subsequent AG50W purifications (IC50; 0.018 mg protein ml-1). As a result of isolations by high performance liquid chromatographies, 16 peptides with the IC50 value of less than 20 μM, composed of 2-7 amino acid residues were identified from the WG hydrolyzate. Judging from the high content (260 mg in 100 g of AG50W fraction) and powerful ACE inhibitory activity (IC50; 0.48 μM), Ile-Val-Tyr was identified as a main contributor to the ACE inhibition of the hydrolyzate.

Original languageEnglish
Pages (from-to)289-297
Number of pages9
JournalJournal of Peptide Science
Volume5
Issue number7
DOIs
Publication statusPublished - Jul 1999

Fingerprint

Enzyme inhibition
Peptidyl-Dipeptidase A
Triticum
Inhibitory Concentration 50
Enzyme activity
Peptides
isoleucyl-valyl-tyrosine
High performance liquid chromatography
Bacilli
Amylases
Purification
Hydrolysis
Proteins
High Pressure Liquid Chromatography
Amino Acids

All Science Journal Classification (ASJC) codes

  • Analytical Chemistry
  • Biochemistry, Genetics and Molecular Biology(all)
  • Biochemistry

Cite this

Preparation and characterization of novel bioactive peptides responsible far angiotensin I-converting enzyme inhibition from wheat germ. / Matsui, Toshiro; Li, Chun Hui; Osajima, Yutaka.

In: Journal of Peptide Science, Vol. 5, No. 7, 07.1999, p. 289-297.

Research output: Contribution to journalArticle

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