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Sequential optimization strategy, based on statistical experimental designs, was employed to enhance the production of uricase by Pseudomonas aeruginosa local isolate. Glucose supplementation to the basal production medium inhibits uricase production, perhaps by catabolic repression. For screening of bioprocess parameters significantly influencing uricase activity, the two-level Plackett–Burman design...
Two different extracellular lipases were isolated and purified from Pseudomonas aeruginosa Ps-x to apparent homogeneity using ammonium sulfate precipitation followed by ion exchange chromatography on Q- and S-Sepharose column. Both of the purified lipases are monomeric protein with molecular weight of 15.5 and 54.97 KDa respectively. The optimal activities of the enzymes were at 45 and 50°C and pHs...
Urate oxidase (uricase) was isolated and purified from Pseudomonas aeruginosa to apparent homogeneity using ammonium sulphate precipitation followed by ion exchange and gel filtration chromatography. The specific activity of the purified uricase enzyme was found to be 636.36 with the use of uric acid as a substrate. The purified uricase enzyme is a monomeric protein with molecular weight of 64 kilodaltons...
In a previous study we reported for the first time the isolation and characterization of urate oxidase enzyme from Pseudomo-nas aeruginosa. In this work we isolated and cloned a 1.350 kilobase DNA fragment that encode a putative urate oxidase gene from the genomic library of P. aeruginosa Ps-x. The nucleotide sequence of the cloned DNA insert revealed an open reading frame that encodes a protein of...
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