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Stabilization of Escherichia coli uridine phosphorylase by evolution and immobilization

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dc.contributor.author Visser, Daniel F
dc.contributor.author Hennessy F
dc.contributor.author Rashamuse J
dc.contributor.author Pletschke B
dc.contributor.author Brady D
dc.date.accessioned 2011-07-19T12:37:05Z
dc.date.available 2011-07-19T12:37:05Z
dc.date.issued 2010-08
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
dc.identifier.uri http://hdl.handle.net/10204/5109
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 - en_ZA


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