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The catalases from marine bacterium Bacillus sp.N2a (BNC) and Acinetobacter sp.YS0810(YS0810CAT) were purified and characterized.BNC from Bacillus sp.N2a isolated from Antarctic seawater has a molecular mass of about 230 kD and is composed of four identical subunits of 56 kD.The catalase showed optimal activity at 25 ℃ and at pH range of 6-11.The enzyme could be inhibited by azide, hydroxylamine and mercaptoethanol.The activation energy of BNC was 13 kJ/mol.The gene of psychrophilic catalase BNC was cloned by degenerate PCR and inverse PCR.