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