Purification and Properties of a Proteinase from a Marine Luminous Bacterium, Vibrio splendidus Strain FLE-2

Abstract

A proteolytic, marine luminous bacterium was isolated from seawater and identified as Vibrio splendidus biotype I strain FLE-2. A proteinase from this strain, with a specific activity 21-fold higher than that of the culture supernatant, was purified to homogeneity. The purified enzyme had a molecular weight of 50,000. The enzyme was most active at pH 8.0 and 55°C, and stable below 35°C. The enzyme activity was completely inhibited by EDTA, orthophenanthrolin and phosphoramidon. Also metal ions such as Cu2+, Hg2+, Ni2+, Cd2+ and Co2+ inhibited the activity. These results indicate that this enzyme is a metal-chelater-sensitive, alkaline proteinase. © 1988, Japan Society for Bioscience, Biotechnology, and Agrochemistry. All rights reserved.