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Sharma NK, Thakur S, Thakur N, et al. Thermostable Xanthine Oxidase Activity from Bacillus pumilus RL-2d Isolated from Manikaran Thermal Spring: Production and Characterization. Indian J Microbiol. 2015;56(1):88-98doi: 10.1007/s12088-015-0547-3.
Sharma, N. K., Thakur, S., Thakur, N., Savitri, & Bhalla, T. C. (2016). Thermostable Xanthine Oxidase Activity from Bacillus pumilus RL-2d Isolated from Manikaran Thermal Spring: Production and Characterization. Indian journal of microbiology, 56(1), 88-98. https://doi.org/10.1007/s12088-015-0547-3
Sharma, Nirmal Kant, et al. "Thermostable Xanthine Oxidase Activity from Bacillus pumilus RL-2d Isolated from Manikaran Thermal Spring: Production and Characterization." Indian journal of microbiology vol. 56,1 (2016): 88-98. doi: https://doi.org/10.1007/s12088-015-0547-3
Sharma NK, Thakur S, Thakur N, Savitri, Bhalla TC. Thermostable Xanthine Oxidase Activity from Bacillus pumilus RL-2d Isolated from Manikaran Thermal Spring: Production and Characterization. Indian J Microbiol. 2016 Mar;56(1):88-98. doi: 10.1007/s12088-015-0547-3. Epub 2015 Aug 21. PMID: 26843701; PMCID: PMC4729748.
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Indian J Microbiol. 2016 Mar;56(1):88-98. doi: 10.1007/s12088-015-0547-3. Epub 2015 Aug 21.

Thermostable Xanthine Oxidase Activity from Bacillus pumilus RL-2d Isolated from Manikaran Thermal Spring: Production and Characterization.

Indian journal of microbiology

Nirmal Kant Sharma, Shikha Thakur, Neerja Thakur, Savitri, Tek Chand Bhalla

Affiliations

  1. Department of Biotechnology, Himachal Pradesh University, Summer Hill, Shimla, Himachal Pradesh 171005 India.

PMID: 26843701 PMCID: PMC4729748 DOI: 10.1007/s12088-015-0547-3

Abstract

Xanthine oxidase is an important enzyme of purine metabolism that catalyzes the hydroxylation of hypoxanthine to xanthine and then xanthine to uric acid. A thermostable xanthine oxidase is being reported from a thermophilic organism RL-2d isolated from the Manikaran (Kullu) hot spring of Himachal Pradesh (India). Based on the morphology, physiological tests, and 16S rDNA gene sequence, RL-2d was identified as Bacillus pumilus. Optimization of physiochemical parameters resulted into 4.1-fold increase in the xanthine oxidase activity from 0.051 U/mg dcw (dry cell weight) to 0.209 U/mg dcw. The xanthine oxidase of B. pumilus RL-2d has exhibited very good thermostability and its t1/2 at 70 and 80 °C were 5 and 1 h, respectively. Activity of this enzyme was strongly inhibited by Hg(2+), Ag(+) and allopurinol. The investigation showed that B. pumilus RL-2d exhibited highest xanthine oxidase activity and remarkable thermostability among the other xanthine oxidases reported so far.

Keywords: Bacillus pumilus; Thermophilic microorganisms; Thermostability; Xanthine oxidase

References

  1. Bioorg Med Chem. 2011 Jan 1;19(1):211-20 - PubMed
  2. J Biol Chem. 1990 Aug 5;265(22):13047-54 - PubMed
  3. Fungal Biol. 2010 May-Jun;114(5-6):387-95 - PubMed
  4. Cardiovasc Ther. 2008 Spring;26(1):59-64 - PubMed
  5. Artif Cells Blood Substit Immobil Biotechnol. 2012 Aug;40(4):275-9 - PubMed
  6. J Chromatogr B Analyt Technol Biomed Life Sci. 2012 Oct 1;906:19-24 - PubMed
  7. Indian J Microbiol. 2015 Dec;55(4):357-65 - PubMed
  8. Indian J Microbiol. 2010 Oct;50(Suppl 1):2-9 - PubMed
  9. BMC Biochem. 2007 May 18;8:8 - PubMed
  10. J Biol Chem. 2008 Feb 22;283(8):4818-24 - PubMed
  11. Biochim Biophys Acta. 2000 Jul 14;1480(1-2):302-10 - PubMed

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