KINETICS OF EXTRACELLULAR PROTEASE FROM THE OBLIGATELY PSYCHROPHILIC VIBRIO OP7 OF FISH ORIGIN

The extracellular protease recovered from the obligately psychrophilic marine Vibrio OP7 of fish origin was able to degrade fish actomyosin at 5-degrees-C. The V(max) and the apparent K(m) values for the enzyme were 33.3-mu-g/ml/min and 2.5 mg/ml, respectively. Ethylenediamine tetracetic acid (EDTA) and sodium tripolyphosphate (TPP) were found to inhibit the enzyme's activity at concentrations of 0.075 mg/ml and 0.25 mg/ml, respectively. EDTA produced a noncompetitive inhibition, whereas TPP produced a mixed of noncompetitive and uncompetitive inhibitions of the enzyme.