title: Enzymatic dehalogenation of pentachlorophenol by Pseudomonas fluorescens of the microbial community from tannery effluent.
abstract: Four different bacterial isolates obtained from a stable bacterial consortium were capable of utilizing pentachlorophenol (PCP) as sole carbon and energy source. The consortium was developed by continuous enrichment in the chemostat. The degradation of PCP by bacterial strain was preceded through an oxidative route as indicated by accumulation of tetrachloro-rho-hydroquinone and dichlorohydroquinone as determined by high performance liquid chromatography (HPLC). Among the four isolates, Pseudomonas fluorescens exhibited maximum degradation capability and enzyme production. PCP-monooxygenase enzyme was extracted from culture extract and fractionated by DEAE-cellulose ion exchange chromatography. The molecular weight of the enzyme, purified from Pseudomonas fluorescens, determined by sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE) and gel filtration chromatography was found to be 24000 Da.
authors.affiliation: Department of Environmental Sciences, College of Basic Sciences and Humanities, G B Pant University of Agriculture and Technology, Qt No 1918, Sector-6, Ta Colony, Pantnagar-263145, Uttaranchal, India.
authors.forename: Shachi
authors.initials: S
authors.lastname: Shah
authors.forename: Indu Shekhar
authors.initials: IS
authors.lastname: Thakur
mesh_terms: D001673:Biodegradation, Environmental; D002851:Chromatography, High Pressure Liquid; D003470:Culture Media; D007194:India; D007220:Industrial Waste; D006899:Mixed Function Oxygenases / Q000302:isolation & purification / Q000378:metabolism*; D010084:Oxidation-Reduction; D010416:Pentachlorophenol / Q000378:metabolism*; D011551:Pseudomonas fluorescens / Q000201:enzymology* / Q000254:growth & development / Q000302:isolation & purification; D013633:Tanning
chemical_list: D003470:Culture Media; D007220:Industrial Waste; D010416:Pentachlorophenol; D006899:Mixed Function Oxygenases; C069781:pentachlorophenol monooxygenase