Polish Journal of Microbiology (Sep 2023)

Cloning, Heterologous Expression, and Characterization of a Neutral Uricase from Arthrobacter sp. CSAJ-16 in Cangshan Mountain

  • Yan Xin,
  • Hu Wei,
  • Zhu Yun-Guo,
  • Liu Qing-Qing,
  • Wang Shuai,
  • Liu Hong-Yan,
  • Zhu Dan,
  • Lv Zhi-Hua,
  • Li Lin-Hua,
  • Yin Yi-Rui

DOI
https://doi.org/10.33073/pjm-2023-027
Journal volume & issue
Vol. 72, no. 3
pp. 277 – 283

Abstract

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Uricase (or Urate oxidase), a key enzyme involved in purine metabolism, is commonly used in treating conditions such as gout, hyperuricemia, and tumor lysis syndrome. In this study, a uricase-producing strain (named CSAJ-16) was isolated from the soil sample of Cangshan Mountain, Yunnan Province, China. This strain was identified as Arthrobacter sp. CSAJ-16. Based on the gene sequence alignment, the uricase gene (named aruox) of Arthrobacter sp. CSAJ-16 was amplified and heterologously expressed. The recombinant uricase (ArUOX) was about 32 kDa. The optimal pH and temperature of ArUOX were pH 7 and 20°C, respectively. The ArUOX remained above 50% relative activity after incubation at 37°C for 100 min or at pH 6.0–8.6 for 24 h. Moreover, metal ions such as K+, Mg2+, Ca2+, Ba2+ and Pb2+ can significantly enhance the activity of ArUOX (> 200%). These enzymatic properties indicate that ArUOX has potential applications in pharmaceutical enzymes and uric acid detection kits.

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