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

A peptide (F^sub 4^) 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 F^sub 4^ was Pro-Ser-Gly-Gln-Tyr-Tyr, having the IC^sub 50^ value of 0.1 mM...

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Veröffentlicht in:	Biotechnology letters 1999-12, Vol.21 (12), p.1055-1058
Hauptverfasser:	SUH, H. J, WHANG, J. H, LEE, H
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino acids angiotensin I Bacillus licheniformis Biological and medical sciences Biotechnology Body weight Corn Enzymes Fundamental and applied biological sciences. Psychology Gluten Health. Pharmaceutical industry Industrial applications and implications. Economical aspects Other active biomolecules peptide F4 Peptides Production of active biomolecules serine proteinase Zea mays
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Zusammenfassung:	A peptide (F^sub 4^) 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 F^sub 4^ was Pro-Ser-Gly-Gln-Tyr-Tyr, having the IC^sub 50^ value of 0.1 mM. The peptide (F^sub 4^), at 30 mg kg^sup -1^ body weight of rat, antagonized the rat's pressor response to angiotensin I.[PUBLICATION ABSTRACT]
ISSN:	0141-5492 1573-6776
DOI:	10.1023/A:1005688627350