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Please use this identifier to cite or link to this item: http://hdl.handle.net/10204/6370

Title: Immobilisation and characterisation of biocatalytic co-factor recycling enzymes, glucose dehydrogenase and NADH oxidase, on aldehyde functional ReSynTM polymer microspheres
Authors: Twala, BV
Sewell, BT
Jordaan, J
Keywords: Immobilisation
Dehydrogenase
Oxidase
ReSynTM
Biocatalysis
Issue Date: Mar-2012
Publisher: Elseveir
Citation: Twala, B.V, Sewell, B.T and Jordaan, J. 2012. Immobilisation and characterisation of biocatalytic co-factor recycling enzymes, glucose dehydrogenase and NADH oxidase, on aldehyde functional ReSynTM polymer microspheres. Enzyme and Microbial Technology, Vol. 50, pp 331-336
Series/Report no.: Workflow;9883
Abstract: The use of enzymes in industrial applications is limited by their instability, cost and difficulty in their recovery and re-use. Immobilisation is a technique which has been shown to alleviate these limitations in biocatalysis. Here we describe the immobilisation of two biocatalytically relevant co-factor recycling enzymes, glucose dehydrogenase (GDH) and NADH oxidase (NOD) on aldehyde functional ReSynTM polymer microspheres with varying functional group densities. The successful immobilisation of the enzymes on this new high capacity microsphere technology resulted in the maintenance of activity of 40% for GDH and a maximum of 15.4% for NOD. The microsphere variant with highest functional group density of ~3500 mol g-1 displayed the highest specific activity for the immobilisation of both enzymes at 33.22 U mg-1 and 6.75 U mg-1 for GDH and NOD with respective loading capacities of 51% (0.51 mg mg-1) and 129% (1.29 mg mg-1). The immobilised GDH further displayed improved activity in the acidic pH range. Both enzymes displayed improved pH and thermal stability with the most pronounced thermal stability for GDH displayed on ReSynTM A during temperature incubation at 65 C with a 13.59 fold increase, and NOD with a 2.25-fold improvement at 45 C on the same microsphere variant. An important finding is the suitability of the microspheres for stabilisation of the multimeric protein GDH.
Description: Copyright: 2012 Elsevier. This is a pre-print version of the work. The definitive version is published in Enzyme and Microbial Technology, Vol. 50, pp 331-336.
URI: http://www.sciencedirect.com/science/article/pii/S0141022912000348
http://hdl.handle.net/10204/6370
ISSN: 0141-0229
Appears in Collections:Enzyme technologies
General science, engineering & technology

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