Li Q, Li L, Kou X F, Zhang S H
Wei Sheng Wu Xue Bao. 1989 Feb;29(1):39-44.
Two strains of Pseudomonus sp. having the extracellular catechol 1, 2-dioxygenase activity were selected from 112 bacterial strains. The conditions for enzyme production of the strains were examined. The optimal temperature and pH for enzyme formation were 30 degrees C and pH 6.8-7.0 respectively. Enzyme formation was enhanced by sodium benzoate, and was markedly inhibited by glucose, maltose and glycerol. Ammoniacal nitrogen sources were essential for cell growth and enzyme production. Sodium succinate was an effective inducer for enzyme formation. When the organism was grown in 0.15% sodium benzoate medium (pH 6.8-7.0) at 30 degrees C for 72 hours, about 10 units of catechol 1,2 dioxygenase per ml was obtained.
从112株细菌中筛选出两株具有胞外儿茶酚1,2 -双加氧酶活性的假单胞菌属菌株。考察了这些菌株的产酶条件。酶形成的最适温度和pH分别为30℃和pH 6.8 - 7.0。苯甲酸钠可增强酶的形成，而葡萄糖、麦芽糖和甘油则对其有显著抑制作用。氨态氮源对细胞生长和产酶至关重要。琥珀酸钠是酶形成的有效诱导剂。当该微生物在30℃的0.15%苯甲酸钠培养基（pH 6.8 - 7.0）中培养72小时时，每毫升可获得约10单位的儿茶酚1,2 -双加氧酶。
