Purification and characterization of thermostable xylose(glucose) isomerase from Bacillus thermoantarcticus View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2001-10

AUTHORS

L Lama, B Nicolaus, V Calandrelli, I Romano, R Basile, A Gambacorta

ABSTRACT

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 Km 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. More... »

PAGES

234-240

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/sj.jim.7000182

DOI

http://dx.doi.org/10.1038/sj.jim.7000182

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1011651177

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/11687936


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