dc.contributor.author |
Rashamuse, KJ
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dc.contributor.author |
Burton, SG
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dc.contributor.author |
Stanfford, WHL
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dc.contributor.author |
Cowan, DA
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dc.date.accessioned |
2009-05-13T09:36:42Z |
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dc.date.available |
2009-05-13T09:36:42Z |
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dc.date.issued |
2007-02 |
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dc.identifier.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 |
en |
dc.identifier.uri |
http://hdl.handle.net/10204/3376
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dc.description |
20th South African society of biochemistry and molecular biology, University of Natal, Pietermarizburg, January 2006 |
en |
dc.description.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 |
en |
dc.language.iso |
en |
en |
dc.subject |
Molecular characterization |
en |
dc.subject |
Family III esterase |
en |
dc.subject |
Burkholderia multivorans |
en |
dc.subject |
UWC10 |
en |
dc.subject |
Penicillin |
en |
dc.subject |
Enzymes |
en |
dc.subject |
Carboxylesterases gene |
en |
dc.subject |
3D model structur |
en |
dc.subject |
DNA |
en |
dc.title |
Molecular characterization of a novel family VIII esterase from burkholderia multivorans UWC10 |
en |
dc.type |
Conference Presentation |
en |
dc.identifier.apacitation |
Rashamuse, K., Burton, S., Stanfford, W., & Cowan, D. (2007). Molecular characterization of a novel family VIII esterase from burkholderia multivorans UWC10. http://hdl.handle.net/10204/3376 |
en_ZA |
dc.identifier.chicagocitation |
Rashamuse, KJ, SG Burton, WHL Stanfford, and DA Cowan. "Molecular characterization of a novel family VIII esterase from burkholderia multivorans UWC10." (2007): http://hdl.handle.net/10204/3376 |
en_ZA |
dc.identifier.vancouvercitation |
Rashamuse K, Burton S, Stanfford W, Cowan D, Molecular characterization of a novel family VIII esterase from burkholderia multivorans UWC10; 2007. http://hdl.handle.net/10204/3376 . |
en_ZA |
dc.identifier.ris |
TY - Conference Presentation
AU - Rashamuse, KJ
AU - Burton, SG
AU - Stanfford, WHL
AU - Cowan, DA
AB - 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
DA - 2007-02
DB - ResearchSpace
DP - CSIR
KW - Molecular characterization
KW - Family III esterase
KW - Burkholderia multivorans
KW - UWC10
KW - Penicillin
KW - Enzymes
KW - Carboxylesterases gene
KW - 3D model structur
KW - DNA
LK - https://researchspace.csir.co.za
PY - 2007
T1 - Molecular characterization of a novel family VIII esterase from burkholderia multivorans UWC10
TI - Molecular characterization of a novel family VIII esterase from burkholderia multivorans UWC10
UR - http://hdl.handle.net/10204/3376
ER -
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en_ZA |