dc.contributor.author |
Visser, Daniel F
|
|
dc.contributor.author |
Hennessy F
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|
dc.contributor.author |
Rashamuse J
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|
dc.contributor.author |
Pletschke B
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|
dc.contributor.author |
Brady D
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|
dc.date.accessioned |
2011-07-19T12:37:05Z |
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dc.date.available |
2011-07-19T12:37:05Z |
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dc.date.issued |
2010-08 |
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dc.identifier.citation |
Visser, DF, Hennessy, F, Rashamuse, J, et al. 2011. Stabilization of Escherichia coli uridine phosphorylase by evolution and immobilization. Journal of Molecular Catalysis B: Enzymatic, Vol. 68(3/4), pp. 279-285 |
en_US |
dc.identifier.issn |
1381-1177 |
|
dc.identifier.uri |
http://www.sciencedirect.com/science/article/pii/S1381117710003012
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|
dc.identifier.uri |
http://hdl.handle.net/10204/5109
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|
dc.description |
Copyright: 2010 Elsevier Publishers. This is a pre print version of the work. The definitive version is published in the Journal of Molecular Catalysis B: Enzymatic, Vol. 68(3/4), pp. 279-285 |
en_US |
dc.description.abstract |
Uridine phosphorylase from Escherichia coli was evolved by iterative saturation mutagenesis. The best mutant showed a temperature optimum of 60C and a half-life of 17.3 h at 60C. The mutant enzyme, as well as a purine nucleoside phosphorylase from Bacillus halodurans, were immobilised as SpherezymesTM. Immobilisation of the mutant enzyme provided a further increase in thermostability. When combined with the purine nucleoside phosphorylase from B. halodurans, productivity of 5-methyluridine, a pharmaceutical intermediate, was increased from 10 to 31 g.l-1.h-1. |
en_US |
dc.language.iso |
en |
en_US |
dc.publisher |
Elsevier Publishers |
en_US |
dc.relation.ispartofseries |
Workflow;4619 |
|
dc.subject |
Biocatalysis |
en_US |
dc.subject |
Transglycosylation |
en_US |
dc.subject |
Directed evolution |
en_US |
dc.subject |
Immobilisation |
en_US |
dc.subject |
Spherezyme |
en_US |
dc.subject |
5-methyluridine |
en_US |
dc.title |
Stabilization of Escherichia coli uridine phosphorylase by evolution and immobilization |
en_US |
dc.type |
Article |
en_US |
dc.identifier.apacitation |
Visser, D. F., Hennessy F, Rashamuse J, Pletschke B, & Brady D (2010). Stabilization of Escherichia coli uridine phosphorylase by evolution and immobilization. http://hdl.handle.net/10204/5109 |
en_ZA |
dc.identifier.chicagocitation |
Visser, Daniel F, Hennessy F, Rashamuse J, Pletschke B, and Brady D "Stabilization of Escherichia coli uridine phosphorylase by evolution and immobilization." (2010) http://hdl.handle.net/10204/5109 |
en_ZA |
dc.identifier.vancouvercitation |
Visser DF, Hennessy F, Rashamuse J, Pletschke B, Brady D. Stabilization of Escherichia coli uridine phosphorylase by evolution and immobilization. 2010; http://hdl.handle.net/10204/5109. |
en_ZA |
dc.identifier.ris |
TY - Article
AU - Visser, Daniel F
AU - Hennessy F
AU - Rashamuse J
AU - Pletschke B
AU - Brady D
AB - Uridine phosphorylase from Escherichia coli was evolved by iterative saturation mutagenesis. The best mutant showed a temperature optimum of 60C and a half-life of 17.3 h at 60C. The mutant enzyme, as well as a purine nucleoside phosphorylase from Bacillus halodurans, were immobilised as SpherezymesTM. Immobilisation of the mutant enzyme provided a further increase in thermostability. When combined with the purine nucleoside phosphorylase from B. halodurans, productivity of 5-methyluridine, a pharmaceutical intermediate, was increased from 10 to 31 g.l-1.h-1.
DA - 2010-08
DB - ResearchSpace
DP - CSIR
KW - Biocatalysis
KW - Transglycosylation
KW - Directed evolution
KW - Immobilisation
KW - Spherezyme
KW - 5-methyluridine
LK - https://researchspace.csir.co.za
PY - 2010
SM - 1381-1177
T1 - Stabilization of Escherichia coli uridine phosphorylase by evolution and immobilization
TI - Stabilization of Escherichia coli uridine phosphorylase by evolution and immobilization
UR - http://hdl.handle.net/10204/5109
ER -
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en_ZA |