Biodegradation of p-nitrophenol by engineered strain

Kinetics of biodegradation of p-nitrophenol by different bacteria.

Three bacterial species, i.e., Ralstonia sp. SJ98, Arthrobacter protophormiae RKJ100, and Burkholderia cepacia RKJ200, have been examined for their efficiency and kinetics behavior toward PNP degradation. All the three bacteria utilized PNP as the sole source of carbon, nitrogen, and energy. The rates of radiolabeled [U-(14)C]PNP degradation by all the bacteria were higher in the nitrogen-free ...

Biodegradation of p-nitrophenol by Immobilized Rhodococcus sp. Strain Y-1

A high efficiency p-nitrophenol (PNP) degrading bacterial strain Y-1 capable of utilizing PNP as sole carbon and energy source was screened and isolated from the activated sludge of Jilin Chemical Plant Oxidation Ditch in China. 16S rDNA sequencing identified strain Y-1 to be Rhodococcus sp. Polyvinyl alcohol (PVA) and sodium alginate were employed to immobilize the Rhodococcus sp. strain Y-1. ...

A Microcosm Study on P-Nitrophenol Biodegradation in Soil Slurry by Alcaligenes faecalis: Plackett-Burman Design

Bioremediation of p-Nitrophenol by Pseudomonas putida 1274 strain

BACKGROUND p-Nitrophenol (PNP) occurs as contaminants of industrial effluents and it is the most important environmental pollutant and causes significant health and environmental risks, because it is toxic to many living organisms. Nevertheless, the information regarding PNP degradation pathways and their enzymes remain limited. OBJECTIVE To evaluate the efficacy of the Pseudomonas Putida 127...

Biodegradation of p-nitrophenol via 1,2,4-benzenetriol by an Arthrobacter sp.

The degradation of p-nitrophenol (PNP) by Moraxella and Pseudomonas spp. involves an initial monooxygenase-catalyzed removal of the nitro group. The resultant hydroquinone is subject to ring fission catalyzed by a dioxygenase enzyme. We have isolated a strain of an Arthrobacter sp., JS443, capable of degrading PNP with stoichiometric release of nitrite. During induction of the enzymes required ...