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Please use this identifier to cite or link to this item: http://hdl.handle.net/10204/4349

Title: Cloning, purification and characterisation of a recombinant purine nucleoside phosphorylase from Bacillus halodurans Alk36
Authors: Visser, DF
Hennessy, F
Rashamuse, KJ
Louw, ME
Brady, D
Keywords: Nucleoside phosphorylase
Biocatalysis
Guanosine
5-Methyluridine
Bacillus halodurans
Issue Date: Mar-2010
Publisher: Springer
Citation: Visser, DF, et al. 2010. Cloning, purification and characterisation of a recombinant purine nucleoside phosphorylase from Bacillus halodurans Alk36 . Extremophiles, Vol. 14(2), pp 185-192
Abstract: A purine nucleoside phosphorylase from the alkaliphile Bacillus halodurans Alk36 has been cloned and over expressed in E. coli. The purified enzyme had a kcat of 2.03 x 10-9 s-1 and a km of 206 µM on guanosine. The optimal pH range was between 5.7 and 8.4, with an optimal temperature of 70ºC and a half life at 60ºC of 20.8 hours.
Description: Copyright: The Author(s) 2010. This article is published with open access at Springerlink.com
URI: http://hdl.handle.net/10204/4349
ISSN: 1431-0651
Appears in Collections:Enzyme technologies
General science, engineering & technology

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