A peptide from corn gluten hydrolysate that is inhibitory toward angiotensin I converting enzyme

Hyung Joo Suh, J. H. Whang, H. Lee

Research output: Contribution to journalArticle

49 Citations (Scopus)

Abstract

A peptide (F4) that inhibits angiotensin I converting enzyme (ACE) was isolated from corn gluten hydrolysate prepared with Pescalase, a serine protease from Bacillus licheniformis. The N-terminal amino acid sequence of F4 was Pro-Ser-Gly-Gln-Tyr-Tyr, having the IC50 value of 0.1 mM. The peptide (F4), at 30 mg kg-1 body weight of rat, antagonized the rat's pressor response to angiotensin I.

Original languageEnglish
Pages (from-to)1055-1058
Number of pages4
JournalBiotechnology Letters
Volume21
Issue number12
DOIs
Publication statusPublished - 1999 Dec 1

Fingerprint

Glutens
Peptidyl-Dipeptidase A
Peptides
Zea mays
Rats
Enzymes
Angiotensin I
Serine Proteases
Bacilli
Inhibitory Concentration 50
Amino acids
Amino Acid Sequence
Body Weight
Amino Acids
Bacillus licheniformis
Peptide Hydrolases

Keywords

  • Angiotensin converting enzyme
  • Corn gluten
  • Peptide inhibitor
  • Pescalase
  • Protease

ASJC Scopus subject areas

  • Biotechnology
  • Bioengineering
  • Applied Microbiology and Biotechnology
  • Microbiology

Cite this

A peptide from corn gluten hydrolysate that is inhibitory toward angiotensin I converting enzyme. / Suh, Hyung Joo; Whang, J. H.; Lee, H.

In: Biotechnology Letters, Vol. 21, No. 12, 01.12.1999, p. 1055-1058.

Research output: Contribution to journalArticle

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