Biotechnology Letters

, Volume 21, Issue 12, pp 1055–1058

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

  • H.J. Suh
  • J.H. Whang
  • H. Lee

DOI: 10.1023/A:1005688627350

Cite this article as:
Suh, H., Whang, J. & Lee, H. Biotechnology Letters (1999) 21: 1055. doi:10.1023/A:1005688627350


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.

angiotensin converting enzyme corn gluten peptide inhibitor Pescalase protease 

Copyright information

© Kluwer Academic Publishers 1999

Authors and Affiliations

  • H.J. Suh
    • 1
  • J.H. Whang
    • 2
  • H. Lee
    • 3
  1. 1.Department of Food and Nutrition, College of Health SciencesKorea UniversitySungbuk-ku, SeoulKorea
  2. 2.Samsung Everland INC.Yongin, Konggi-doKorea
  3. 3.Department of Food and BiotechnologyKyonggi UniversitySuwon, Konggi-doKorea

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