An unusual feruloyl esterase belonging to family VIII esterases and displaying a broad substrate range

Show simple item record Ohlhoff, Colin W. Kirby, Bronwyn M. Casanueva, Ana Huddy, Robert J. Bauer, Rolene Mutepfa, David L.R. Cowan, Don A. Tuffin, Marla I. 2015-07-16T06:07:37Z 2015-07-16T06:07:37Z 2015-08
dc.description.abstract A thermophilic compost metagenomic library constructed in Escherichia coli was functionally screenedfor novel esterases. Of the 110,592 fosmid clones screened, 25 clones demonstrated degradative activ-ity on glyceryl tributyrate (a hit rate of 1:4,423). Four clones displayed ferulic acid esterase activityand were sequenced using 454 Titanium sequencing technology. EstG34, a 410 amino acid protein, wasidentified as having high sequence identity with a number of bacterial -lactamases. EstG34 has theS-X-X-K motif which is conserved in class C -lactamases and family VIII carboxylesterases. Purifiedrecombinant EstG34 had a molecular mass of 42 kDa and displayed hydrolytic activity towards a vari-ety of p-nitrophenyl esters, hydroxycinnamic acid esters and -naphthol acetate. EstG34 represents thefirst family VIII carboxylesterase and -lactamase fold enzyme, able to hydrolyse ferulate and a numberof other hydroxycinnamic acid esters. In addition, EstG34 is the first reported FAE to not adopt the / hydrolase conformation. The sequence similarity and wide substrate utilization capability of this esterasecomplicates its placement within current classification systems, but also draws attention to the enzyme’spotential versatility. en_ZA
dc.description.embargo 2016-08-31 en_ZA
dc.description.librarian hb2015 en_ZA
dc.description.sponsorship The National Research Foundation (NRF) and the Technology Innovation Agency (TIA), South Africa(Project number PB99/08). en_ZA
dc.description.uri en_ZA
dc.identifier.citation Ohlhoff, CW, Kirby, BM, Van Zyl, L, Mutepfa, DLR, Casanueva, A, Huddy, RJ, Bauer, R, Cowan, DA & Tuffin, MI 2015, 'An unusual feruloyl esterase belonging to family VIII esterases and displaying a broad substrate range', Journal of Molecular Catalysis B: Enzymati, vol. 118, pp. 79-88. en_ZA
dc.identifier.issn 1381-1177 (print)
dc.identifier.issn 1873-3158 (online)
dc.identifier.other 10.1016/j.molcatb.2015.04.010
dc.language.iso en en_ZA
dc.publisher Elsevier en_ZA
dc.rights © 2015 Published by Elsevier B.V. Notice : this is the author’s version of a work that was accepted for publication in Journal of Molecular Catalysis B : Enzymatic. Changes resulting from the publishing process, such as peer review, editing, corrections, structural formatting, and other quality control mechanisms may not be reflected in this document. Changes may have been made to this work since it was submitted for publication. A definitive version was subsequently published in Journal of Molecular Catalysis B : Enzymatic, vol. 118, pp. 79-88, 2015. doi :10.1016/j.molcatb.2015.04.010 en_ZA
dc.subject Metagenome en_ZA
dc.subject Alkaliphilic en_ZA
dc.subject Feruloyl Esterase en_ZA
dc.subject Family VIII carboxylesterase en_ZA
dc.title An unusual feruloyl esterase belonging to family VIII esterases and displaying a broad substrate range en_ZA
dc.type Postprint Article en_ZA

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