The gene of catechol 1, 2-dioxygenase was identified and cloned from the genome of Oceanimonas marisflavi 102-Na3. The protein was expressed in Escherichia coli BL21 (DE3) and purified to homogeneity of a dimer with molecular mass of 69.2 kDa. The enzyme was highly stable in pH 6.0–9.5 and below 45 °C and exhibited the maximum activity at pH 8.0 and 30 °C. Being the first characterized intradiol dioxygenase from marine bacteria Oceanimonas sp., the enzyme showed catalytic activity for catechol, 3-methylcatechol, 4-methylcatechol, 3-chlorocatechol, 4-chlorocatechol and pyrogallol. For catechol, K_m and V_max were 11.2 μM and 13.4 U/mg of protein, respectively. The enzyme also showed resistance to most of the metal ions, surfactants and organic solvents, being a promising biocatalyst for biodegradation of aromatic compounds in complex environments.

从Oceanimonas marisflavi 102-Na3基因组中鉴定并克隆了儿茶酚 1, 2-双加氧酶基因。该蛋白质在大肠杆菌BL21 (DE3) 中表达并纯化为均质的二聚体，分子量为 69.2 kDa。该酶在 pH 6.0-9.5 和 45°C 以下高度稳定，在 pH 8.0 和 30°C 时表现出最大活性。作为来自海洋细菌Oceanimonas sp.的第一个表征的内二醇双加氧酶，该酶对儿茶酚、3-甲基儿茶酚、4-甲基儿茶酚、3-氯儿茶酚、4-氯儿茶酚和连苯三酚具有催化活性。对于儿茶酚，K _m和V _max分别为 11.2 μM 和 13.4 U/mg 蛋白质。该酶还表现出对大多数金属离子、表面活性剂和有机溶剂的耐受性，是一种很有前途的生物催化剂，可用于复杂环境中芳香族化合物的生物降解。