Kinetics of extracellular protease from the obligately psychrophilic vibrio OP7 of fish origin

Abstract

The extracellular protease recovered from the obligately psychrophilic marine Vibrio OP7 of fish origin was able to degrade fish actomyosin at 5°C. The Vmax and the apparent Km values for the enzyme were 33.3 μg/ml/min and 2.5 mg/ml, respectively. Ethylenediamine tetracetic acid (EDTA) and sodium tri-polyphosphate (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.