Abstract
A proteinase from the culture supernatant of marine luminous bacterium, Vibrio harveyi strain FLN-77, was purified. The purified enzyme had a molecular weight of 62000. The enzyme was most active at pH 8.0 and 55°C, and was stable below 45°C. The enzyme activity was completely inhibited by ethylendiaminetetra acetic acid, orthophenanthroline and phosphoramidon. Metal ions such as Cu2+, Hg2+ and Ni2+ also inhibited the activity. These results indicated that this enzyme is a metal-chelator-sensitive, alkaline proteinase.
