Characterization of urethanase from Micrococcus species associated with the marine sponge (Spirastrella species)

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Eighty per cent of the urethanase activity of Micrococcus sp. isolated from the marine sponge Spirastrella sp. was cell associated. The urethanase had optimal activity at pH 5.0 and 45°C. The activation and deactivation energies of the partially purified enzyme, calculated from an Arrhenius plot, were 9.31 and 34.01 kcal mol−1, respectively. The enzyme was not affected by EDTA and the major cations of sea water, such as Ca2+, Mg2+ and Na+. The enzyme was resistant to 20% (v/v) ethanol and may be practically applicable in the removal of urethane from alcoholic beverages.

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