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

研究成果: Contribution to journalArticle査読

184 被引用数 (Scopus)

抄録

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.

本文言語英語
ページ(範囲)922-925
ページ数4
ジャーナルBioscience, biotechnology, and biochemistry
57
6
DOI
出版ステータス出版済み - 1993

All Science Journal Classification (ASJC) codes

  • バイオテクノロジー
  • 分析化学
  • 生化学
  • 応用微生物学とバイオテクノロジー
  • 分子生物学
  • 有機化学

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