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


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Abstract

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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