Kinetics of Extracellular Protease From the Obligately Psychrophilic Vibrio OP7 of Fish Origin

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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 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.

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