Properties of the Proteinase from a Luminous Bacterium, Vibrio splendidus ATCC 33125

• Published in: Chemical & pharmaceutical bulletin Vol. 37; no. 5; pp. 1372 - 1374
• Main Authors: FUKASAWA, Shigeki, TAKAGI, Ken, KURATA, Munetsugu
• Format: Journal Article
• Language: English
• Published: Tokyo The Pharmaceutical Society of Japan 1989; Maruzen
• Subjects: Analytical, structural and metabolic biochemistry; biochemical analysis; Biological and medical sciences; chemical extraction; enzymatic activity; enzymes; Enzymes and enzyme inhibitors; Fundamental and applied biological sciences. Psychology; Hydrolases; inhibitors; luminous bacterium; Marine; marine bacterium; molecular weight; proteinase; Vibrio splendidus; Alkaline proteinase; Purification; Gel electrophoresis; Enzyme; Enzyme inhibitor; Metal Ions; Molecular weight; Thermal stability; Gel permeation chromatography; Ion exchange chromatography; Marine environment; Enzymatic activity; Bacteria; Vibrionaceae; Physicochemical properties; Vibrio
• ISSN: 0009-2363; 1347-5223
• DOI: 10.1248/cpb.37.1372

A proteinase was purified from the culture supernatant of a marine luminous bacterium, Vibrio splendidus ATCC 33125. The purified enzyme had a molecular weight of 60000. The enzyme was most active at pH 9.0 and 57°C, and was stable below 45°C. The enzyme activity was inhibited by phosphoramidon, ethylenediaminetetraacetic acid and orthophenanthroline. Metal ions such as Cu2+, Hg2+ and Ni2+ also inhibited the activity. These results indicate that this enzyme is a metal-chelator-sensitive, alkaline proteinase.