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Please use this identifier to cite or link to this item: http://hdl.handle.net/10204/3376

Title: Molecular characterization of a novel family VIII esterase from burkholderia multivorans UWC10
Authors: Rashamuse, KJ
Burton, SG
Stanfford, WHL
Cowan, DA
Keywords: Molecular characterization
Family III esterase
Burkholderia multivorans
UWC10
Penicillin
Enzymes
Carboxylesterases gene
3D model structur
DNA
Issue Date: Feb-2007
Citation: Rashamuse, KJ, Burton, SG, Stanfford, WHL and Cowan, DA. 2006. Molecular characterization of a novel family VIII esterase from burkholderia multivorans UWC10. 20th South African society of biochemistry and molecular biology, University of Natal, Pietermarizburg, January 2006, pp 1
Abstract: An esterase producing Burkholderia multivorans UWC10 strain was isolated by culture enrichment. A shotgun library of B. multivorans UWC10 genomic DNA was screened for esterase activity and a recombinant clone conferring an esterolytic phenotype was identified. Full-length sequencing of the DNA insert showed that it consisted of a single open reading frame (ORF1) encoding a predicted protein of 398 amino acids. ORF1 (termed EstBL) had a high protein sequence identity to family VIII esterases. The EstBL primary structure showed two putative serine motifs, G-V-S149-D-G and S74-V-T-K. The estBL gene was successfully over-expressed in E. coli and the encoded protein purified by a combination of ammonium sulphate fractionation, hydrophobic interaction, ion exchange and size exclusion chromatographies. Biochemical assays confirmed EstBL esterase activity and revealed a preference for short-chain p-nitrophenyl and beta-naphthyl esters (C2-C4) with no activity against beta-lactam substrates. Secondary structure predictions indicated that EstBL adopts the alpha/beta fold, which is common to all esterases
Description: 20th South African society of biochemistry and molecular biology, University of Natal, Pietermarizburg, January 2006
URI: http://hdl.handle.net/10204/3376
Appears in Collections:General science, engineering & technology
Agroprocessing and chemical technology

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