Some Properties of Two Proteinases from a Luminous Bacterium, Vibrio harveyi Strain FLN-108

Abstract

Two proteinases (I and II) from a marine luminous bacterium, FLN-108, were purified to homogeneity. The molecular weights of proteinases I and II were estimated to be 49,000 and 46,000, comprising a dimer of 23,000 molecular weight subunits, respectively. These enzymes were most active at from pH 8.0 to pH 9.0 and 50°C, and stable below 45°C. These enzyme activities were inhibited by EDTA and orthophenanthrolin. Phosphoramidon inhibited the activity of proteinase II, but not that of proteinase I. Metal ions such as Cu²⁺ , Hg²⁺ , and Ni²⁺ strongly inhibited these activities. These results indicate that the proteinases I and II are metal-chelater-sensitive, alkaline proteinases.