Xylose isomerase produced by Bacillus thermoantarcticus was purified 73-fold to homogeneity and its biochemical properties were determined. It was a homotetramer with a native molecular mass of 200 kDa and a subunit molecular mass of 47 kDa, with an isoelectric point at 4.8. The enzyme had a K m of 33 mM for xylose and also accepted D-glucose as substrate. Arrhenius plots of the enzyme activity of xylose isomerase were linear up to a temperature of 85°C. Its optimum pH was around 7.0, and it had 80% of its maximum activity at pH 6.0. This enzyme required divalent cations for its activity and thermal stability. Mn2+, Co2+ or Mg2+ were of comparable efficiency for xylose isomerase reaction, while Mg2+ was necessary for glucose isomerase reaction. Journal of Industrial Microbiology & Biotechnology (2001) 27, 234–240.
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Received 18 March 2001/ Accepted in revised form 03 July 2001
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Lama, L., Nicolaus, B., Calandrelli, V. et al. Purification and characterization of thermostable xylose(glucose) isomerase from Bacillus thermoantarcticus . J Ind Microbiol Biotech 27, 234–240 (2001). https://doi.org/10.1038/sj.jim.7000182
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DOI: https://doi.org/10.1038/sj.jim.7000182