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dc.contributor.author Y. H. en_US
dc.contributor.author A. H. en_US
dc.contributor.author T. H. en_US
dc.date.accessioned 2009-11-20T09:34:24Z
dc.date.available 2009-11-20T09:34:24Z
dc.date.issued 2001-02-01 en_US
dc.identifier http://dx.doi.org/10.1016/S0141-0229(00)00305-7 en_US
dc.identifier.citation Guan , Y H , Brook , A H & Lilley , T H 2001 , ' Production of immobilized penicillin acylase using aqueous polymer systems for enzyme purification and in situ immobilization ' Enzyme and Microbial Technology , vol 28 , no. 2-3 , pp. 2-3 . , 10.1016/S0141-0229(00)00305-7 en_US
dc.identifier.other PURE: 129206 en_US
dc.identifier.other dspace: 2160/3564 en_US
dc.identifier.uri http://hdl.handle.net/2160/3564
dc.description.abstract A novel approach for the isolation and purification of penicillin acylase (PA), which couples aqueous two-phase partitioning and enzyme immobilization has been investigated. A PA yield of 90% was achieved by treating E. coli cells with 4% butyl acetate, freeze-thawing step, and pressure homogenization. PA purification (93% recovery) was achieved by (1) removing cell debris via precipitation with polyethylene glycol (PEG 2000); (2) aqueous two-phase partitioning using a PEG 2000 + phosphate system (87% recovery). An in situ enzyme immobilization approach, using oxirane acrylic or aldehyde-agarose beads dispersed in the PEG-rich phase, was explored for the conversion of penicillin G to 6-aminopenicillanic acid. An appropriate immobilization reaction time was found. The catalytic performance of the enzyme, when immobilized, was found not to be affected by recycling of the phase-forming components. en_US
dc.format.extent 2 en_US
dc.relation.ispartof Enzyme and Microbial Technology en_US
dc.title Production of immobilized penicillin acylase using aqueous polymer systems for enzyme purification and in situ immobilization en_US
dc.contributor.pbl Aberystwyth University en_US
dc.contributor.pbl Institute of Biological, Environmental and Rural Sciences en_US


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