A novel cold active esterase from a deep sea sponge Stelletta normani metagenomic library

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dc.contributor.author Borchert, Erik
dc.contributor.author Selvin, Joseph
dc.contributor.author Kiran, Seghal G.
dc.contributor.author Jackson, Stephen A.
dc.contributor.author O'Gara, Fergal
dc.contributor.author Dobson, Alan D. W.
dc.date.accessioned 2017-10-18T09:40:15Z
dc.date.available 2017-10-18T09:40:15Z
dc.date.issued 2017
dc.identifier.citation Borchert, E., Selvin, J., Kiran, S. G., Jackson, S. A., O'Gara, F. and Dobson, A. D. W. (2017) 'A novel cold active esterase from a deep sea sponge Stelletta normani metagenomic library', Frontiers in Marine Science, 4, 287 (13pp). doi: 10.3389/fmars.2017.00287 en
dc.identifier.volume 4
dc.identifier.startpage 1
dc.identifier.endpage 13
dc.identifier.issn 2296-7745
dc.identifier.uri http://hdl.handle.net/10468/4898
dc.identifier.doi 10.3389/fmars.2017.00287
dc.description.abstract Esterases catalyze the hydrolysis of ester bonds in fatty acid esters with short-chain acyl groups. Due to the widespread applications of lipolytic enzymes in various industrial applications, there continues to be an interest in novel esterases with unique properties. Marine ecosystems have long been acknowledged as a significant reservoir of microbial biodiversity and in particular of bacterial enzymes with desirable characteristics for industrial use, such as for example cold adaptation and activity in the alkaline pH range. We employed a functional metagenomic approach to exploit the enzymatic potential of one particular marine ecosystem, namely the microbiome of the deep sea sponge Stelletta normani. Screening of a metagenomics library from this sponge resulted in the identification of a number of lipolytic active clones. One of these encoded a highly, cold-active esterase 7N9, and the recombinant esterase was subsequently heterologously expressed in Escherichia coli. The esterase was classified as a type IV lipolytic enzyme, belonging to the GDSAG subfamily of hormone sensitive lipases. Furthermore, the recombinant 7N9 esterase was biochemically characterized and was found to be most active at alkaline pH (8.0) and displays salt tolerance over a wide range of concentrations. In silico docking studies confirmed the enzyme's activity toward short-chain fatty acids while also highlighting the specificity toward certain inhibitors. Furthermore, structural differences to a closely related mesophilic E40 esterase isolated from a marine sediment metagenomics library are discussed. en
dc.description.sponsorship Marine Institute (Beaufort Marine Research Award (Sea Change Strategy and the Strategy for Science Technology and Innovation (2006–2012); Marine Research Sub-Programme of the National Development Plan 2007–2013). en
dc.format.mimetype application/pdf en
dc.language.iso en en
dc.publisher Frontiers Media en
dc.relation.uri https://www.frontiersin.org/articles/10.3389/fmars.2017.00287/full
dc.rights © 2017, Borchert, Selvin, Kiran, Jackson, O'Gara and Dobson. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms en
dc.rights.uri https://creativecommons.org/licenses/by/4.0/
dc.subject Cold active esterase en
dc.subject Metagenomic library en
dc.subject Deep sea sponge en
dc.title A novel cold active esterase from a deep sea sponge Stelletta normani metagenomic library en
dc.type Article (peer-reviewed) en
dc.internal.authorcontactother Alan Dobson, Microbiology, University College Cork, Cork, Ireland. +353-21-490-3000 Email: a.dobson@ucc.ie en
dc.internal.availability Full text available en
dc.description.version Published Version en
dc.contributor.funder Marine Institute
dc.contributor.funder Seventh Framework Programme
dc.description.status Peer reviewed en
dc.identifier.journaltitle Frontiers in Marine Science en
dc.internal.IRISemailaddress a.dosbon@ucc.ie en
dc.identifier.articleid 287
dc.relation.project info:eu-repo/grantAgreement/EC/FP7::SP1::KBBE/312184/EU/Increasing Value and Flow in the Marine Biodiscovery Pipeline/PHARMASEA
dc.relation.project info:eu-repo/grantAgreement/EC/FP7::SP3::PEOPLE/607786/EU/BluePharmTrain/BLUEPHARMTRAIN


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© 2017, Borchert, Selvin, Kiran, Jackson, O'Gara and Dobson. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms Except where otherwise noted, this item's license is described as © 2017, Borchert, Selvin, Kiran, Jackson, O'Gara and Dobson. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms
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