ArticleBrazilian journal of microbiology : [publication of the Brazilian Society for Microbiology]2026
Extracellular urate oxidase from Arthrobacter creatinolyticus SA1: statistical optimization, purification, and in-vitro evaluation of antihyperuricemic activity.
Article in Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology], 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Urate oxidase (uricase; EC 1.7.3.3) catalyzes the oxidation of uric acid to allantoin, a highly soluble metabolite that is readily excreted. Lack of functional urate oxidase in human's leads to hyperuricemia, which is associated with gout, tumor lysis syndrome and renal complications. The present study reports statistical optimization, purification, and comprehensive characterization of a novel extracellular urate oxidase secreted by Arthrobacter creatinolyticus SA1. Plackett-Burman Design screening followed by Central Composite Design identified inoculum volume, initial pH, peptone, and yeast extract as key determinants for enzyme production. Under optimized conditions, the enzyme yield 36.18 IU/mL was obtained. The enzyme was purified by ammonium sulfate fractionation and DEAE-Sepharose chromatography with an overall purification of 5.8-fold. SDS-PAGE revealed a 30 kDa subunit, while native-PAGE indicated a homo-tetrameric enzyme with an estimated molecular weight of 120 kDa. The purified enzyme displayed optimal activity at pH 9.0 and 30 °C. The K
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