Inhibition of Angiotensin I-converting Enzyme by Bacillus licheniformis Alkaline Protease Hydrolyzates Derived from Sardine Muscle

Toshiro Matsui, Hiroshi Matsufuji, Masatoshi Nakashima, Yutaka Osajima, Eiji Seki, Katsuhiro Osajima

Research output: Contribution to journalArticle

180 Citations (Scopus)

Abstract

Hydrolyzates which inhibit the angiotensin I-converting enzyme (ACE) were prepared from sardine muscle by Bacillus licheniformis alkaline protease. Considering the practical application of preparations as a functional food material, the best proteolytic conditions with respect to taste, solubility and ACE inhibitory activity were a 0.3 wt% addition of the enzyme and 17-h proteolysis at 50°C and pH 9.0. The preparations under these conditions had potent activity (IC50=0.26 mg protein/ml). Fractionation of the preparations on an ODS column with ethanol resulted in the production of more potent inhibitors. The most potent activity was obtained when eluting with 10% ethanol (IC50=0.015 mg protein/ml). This fraction was apparently rich in acidic amino acids, poor in hydrophobic ones, and effective for use as a physiologically functional food material by virtue of little bitterness, a fish odor and powerful ACE inhibitory activity.

Original languageEnglish
Pages (from-to)922-925
Number of pages4
JournalBioscience, biotechnology, and biochemistry
Volume57
Issue number6
DOIs
Publication statusPublished - Jan 1 1993

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Analytical Chemistry
  • Biochemistry
  • Applied Microbiology and Biotechnology
  • Molecular Biology
  • Organic Chemistry

Fingerprint Dive into the research topics of 'Inhibition of Angiotensin I-converting Enzyme by Bacillus licheniformis Alkaline Protease Hydrolyzates Derived from Sardine Muscle'. Together they form a unique fingerprint.

  • Cite this