Characterization of catechol 1,2-dioxygenase from cell extracts of Sphingomonas xenophaga QYY  

作　　者：M.Salah Uddin 

机构地区：[1]Department of Genetics and Breeding, University of Rajshahi,Rajshahi-6205, Bangladesh

出　　处：《Science China Chemistry》2009年第5期615-620,共6页中国科学（化学英文版）

基　　金：Supported by the National Natural Science Foundation of China (Grant No. 50608011);the 39th Postdoctoral Funds of China (Grant No. 20060390983)

摘　　要：Sphingomonas xenophaga QYY, capable of growing significantly on more than ten kinds of aromatic compounds as sole carbon source, was used to study characterization of catechol 1,2-dioxygenase (C12O) in cell extracts. Characterization of the crude C12O showed that the maximum activity was obtained at 40–70°C and pH 7.8–8.8. Metal ions had different influences on the activity of crude C12O. It was suggested that strain QYY possessed an inducible and ferric-dependent C12O. Kinetic studies showed that the value of V max and K m was 0.25 μmol catechol/L/mg protein/min and 52.85 μmol/L, respectively. In addition, the partial purification of C12O was achieved by a HiTrap Q Sepharose column chromatography.Sphingomonas xenophaga QYY, capable of growing significantly on more than ten kinds of aromatic compounds as sole carbon source, was used to study characterization of catechol 1,2-dioxygenase (C12O) in cell extracts. Characterization of the crude C12O showed that the maximum activity was obtained at 40-70℃ and pH 7.8-8.8. Metal ions had different influences on the activity of crude C12O. It was suggested that strain QYY possessed an inducible and ferric-dependent C12O. Kinetic studies showed that the value of Vmax and Km was 0.25 μmol catechol/L/mg protein/min and 52.85 μmol/L, respectively. In addition, the partial purification of C12O was achieved by a HiTrap Q Sepharose column chromatography.

关 键 词：CATECHOL 1 2-dioxygenase CELL EXTRACTS CHARACTERIZATION SPHINGOMONAS xenophaga 

分 类 号：X503[环境科学与工程—环境工程]