Isolation and characterization of monochloroacetic acid-degrading bacteria

The Journal of General and Applied Microbiology

Tadafumi Horisaki²  Hisakazu Yamane²  Kaori Sumiya²  Tetsuo Takemura¹  Hideaki Nojiri²  Eiko Yoshida² 

[1] Department of Chemistry, Faculty of Science, Tokyo University of Science;Biotechnology Research Center, The University of Tokyo

关键词: Burkholderia;    degradation;    dehalogenase;    monochloroacetic acid;    substrate specificity;   

DOI  :  10.2323/jgam.57.277

学科分类：微生物学和免疫学

来源: Applied Microbiology, Molecular and Cellulrar Biosciences Research Foundation

【 摘 要 】

Five Burkholderia strains (CL-1, CL-2, CL-3, CL-4, and CL-5) capable of degrading monochloroacetic acid (MCA) were isolated from activated sludge or soil samples gathered from several parts of Japan. All five isolates were able to grow on MCA as the sole source of carbon and energy, and argentometry and gas chromatography-mass spectroscopy analyses showed that these five strains consumed MCA completely and released chloride ions stoichiometrically within 25 h. The five isolates also grew on monobromoacetic acid, monoiodoacetic acid, and L-2-monochloropropionic acid as sole sources of carbon and energy. In addition, the five isolates could not grow with DCA but dehalogenate single chlorine from DCA. Because PCR analyses revealed that all five isolates have an identical group II dehalogenase gene fragment and no group I deh gene, only strain CL-1 was analyzed further. The partial amino acid sequence of the group II dehalogenase of strain CL-1, named DehCL1, showed 74.6% and 65.2% identities to corresponding regions of the two MCA dehalogenases, DehCI from Pseudomonas sp. strain CBS-3 and Hdl IVa from Burkholderia cepacia strain MBA4, respectively. The secondary-structure motifs of the haloacid dehalogenase (HAD) superfamily and the amino acid residues involved in substrate binding, catalysis, and hydrophobic pocket formation were conserved in the partial amino acid sequence of DehCL1.

【 授权许可】

Unknown