Purification and kinetics of gelatinase obtained from an obligately psychrophilic marine vibrio Public Deposited

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  • Optimum growth of Marine Psychrophile 41 (MP-41) an obligately psychrophilic marine vibrio, occurred at 18 C and pH 8.0 to pH 8.3. Twenty eight-fold purification of gelatinase from this organism was effected by ammonium sulfate fractionation and column chromatography on Sephadex G-200 gel. The effects of temperature, pH, pressure, and salt concentration were determined for various degrees of enzyme purity and for cells. Differences occurred in the various enzyme preparations with optimal purified gelatinase activity observed at 40 C and pH 9.3. Increasing pressures and salt concentrations decreased the activity of purified gelatinase but salt-free purified gelatinase displayed no activity. The rate of hydrolysis was greater at 40 C than at 5 C. At the lowest gelatinase and gelatin concentrations studied, 0.025 mg/ml and 1 mg/ml respectively, activity was observed although. optimal activity occurred at higher concentrations. Ammonium sulfate was shown to increase the activity of purified gelatinase two-fold.
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