Identification of an esterase isolated using metagenomic technology which displays an unusual substrate scope and its characterisation as an enantioselective biocatalyst

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dc.contributor.authorGavin, Declan P.
dc.contributor.authorMurphy, Edel J.
dc.contributor.authorFoley, Aoife M.
dc.contributor.authorCastilla, Ignacio Abreu
dc.contributor.authorReen, F. Jerry
dc.contributor.authorWoods, David F.
dc.contributor.authorCollins, Stuart G.
dc.contributor.authorO'Gara, Fergal
dc.contributor.authorMaguire, Anita R.
dc.contributor.funderIrish Research Councilen
dc.contributor.funderScience Foundation Irelanden
dc.contributor.funderSeventh Framework Programmeen
dc.contributor.funderDepartment of Agriculture, Food and the Marineen
dc.contributor.funderFood Institutional Research Measureen
dc.contributor.funderHealth Research Boarden
dc.contributor.funderIrish Thoracic Societyen
dc.contributor.funderCystic Fibrosis Foundationen
dc.date.accessioned2019-02-26T15:33:16Z
dc.date.available2019-02-26T15:33:16Z
dc.date.issued2019-02-11
dc.date.updated2019-02-25T16:41:25Z
dc.description.abstractEvaluation of an esterase annotated as 26D isolated from a marine metagenomic library is described. Esterase 26D was found to have a unique substrate scope, including synthetic transformations which could not be readily effected in a synthetically useful manner using commercially available enzymes. Esterase 26D was more selective towards substrates which had larger, more sterically demanding substituents (i.e. iso‐propyl or tert‐butyl groups) on the β‐carbon, which is in contrast to previously tested commercially available enzymes which displayed a preference for substrates with sterically less demanding substituents (i.e. methyl group) at the β‐carbon.en
dc.description.sponsorshipIrish Research Council (EPSPG/2016/41); Enterprise Ireland (CF-2017-0757-P; IP-2015-0390); Department of Agriculture, Food and the Marine ((FIRM 11/F009/MabS; FIRM 13/F/516); (BEAU/BIOD/01)); Irish Research Council for Science, Engineering and Technology (GOIPG/2014/647); Health Research Board and Irish Thoracic Society (MRCG-2014-6)en
dc.description.statusPeer revieweden
dc.description.versionAccepted Versionen
dc.format.mimetypeapplication/pdfen
dc.identifier.citationGavin, D. P., Murphy, E. J., Foley, A. M., Abreu Castilla, I., Reen, F. J., Woods, D. F., Collins, S. G., O'Gara, F. and Maguire, A. (2019) 'Identification of an Esterase Isolated Using Metagenomic Technology which Displays an Unusual Substrate Scope and its Characterisation as an Enantioselective Biocatalyst', Advanced Synthesis & Catalysis, In Press, doi: 10.1002/adsc.201801691en
dc.identifier.doi10.1002/adsc.201801691
dc.identifier.endpage12en
dc.identifier.issn1615-4150
dc.identifier.journaltitleAdvanced Synthesis & Catalysisen
dc.identifier.startpage1en
dc.identifier.urihttps://hdl.handle.net/10468/7543
dc.language.isoenen
dc.publisherWileyen
dc.relation.projectinfo:eu-repo/grantAgreement/SFI/SFI Research Centres/12/RC/2275/IE/Synthesis and Solid State Pharmaceutical Centre (SSPC)/en
dc.relation.projectinfo:eu-repo/grantAgreement/EC/FP7::SP3::PEOPLE/607786/EU/BluePharmTrain/BLUEPHARMTRAINen
dc.relation.projectinfo:eu-repo/grantAgreement/EC/FP7::SP1::KBBE/312184/EU/Increasing Value and Flow in the Marine Biodiscovery Pipeline/PHARMASEAen
dc.relation.projectinfo:eu-repo/grantAgreement/EC/FP7::SP1::KBBE/311975/EU/Marine Microorganisms: Cultivation Methods for Improving their Biotechnological Applications/MACUMBAen
dc.relation.projectinfo:eu-repo/grantAgreement/EC/FP7::SP1::KBBE/287589/EU/Marine Microbial Biodiversity, Bioinformatics and Biotechnology/MICRO B3en
dc.relation.projectinfo:eu-repo/grantAgreement/EC/H2020::IA/634486/EU/Industrial Applications of Marine Enzymes: Innovative screening and expression platforms to discover and use the functional protein diversity from the sea/INMAREen
dc.relation.projectinfo:eu-repo/grantAgreement/SFI/SFI Research Centres/12/RC/2275/IE/Synthesis and Solid State Pharmaceutical Centre (SSPC)/en
dc.relation.projectinfo:eu-repo/grantAgreement/SFI/SFI Technology and Innovation Development Award (TIDA) - Training Award/13/TIDA/B2625 TIDA Training 2014/IE/Small molecule inhibitors of HIF-1: a new class of anti-cancer therapeutics./en
dc.relation.projectinfo:eu-repo/grantAgreement/SFI/SFI Technology and Innovation Development Award (TIDA)/12/TIDA/B2411/IE/Development of small molecule therapeutics for medical intervention: anti-biofilm inhibitors for the medical device sector./en
dc.relation.projectinfo:eu-repo/grantAgreement/SFI/SFI Technology and Innovation Development Award (TIDA)/12/TIDA/B2405/IE/Optimised detection of key biomarkers of Pseudomonas aeruginosa towards a clinical application/en
dc.relation.projectinfo:eu-repo/grantAgreement/SFI/SFI Technology and Innovation Development Award (TIDA)/14/TIDA/2438/IE/Next Generation Antibiotics: anti-biofilm, anti-pathogenic natural bioactives from marine microorganisms./en
dc.relation.projectinfo:eu-repo/grantAgreement/SFI/SFI Technology and Innovation Development Award (TIDA)/15/TIDA/2977/IE/Pre-clinical testing of novel fungal biofilm blockers for the medical device sector./en
dc.relation.projectinfo:eu-repo/grantAgreement/SFI/SFI Research Frontiers Programme (RFP)/09/RFP/BMT2350/IE/An investigation of the molecular interactions between statins and microbial pathogens and their combined impact on the human immune response./en
dc.relation.urihttps://onlinelibrary.wiley.com/doi/abs/10.1002/adsc.201801691
dc.rights© 2019 WILEY‐VCH Verlag GmbH & Co. KGaA, Weinheim. This is the peer reviewed version of the following article: (2019), Identification of an Esterase Isolated Using Metagenomic Technology which Displays an Unusual Substrate Scope and its Characterisation as an Enantioselective Biocatalyst. Adv. Synth. Catal., Accepted Author Manuscript, which has been published in final form at https://doi.org/10.1002/adsc.201801691. This article may be used for non-commercial purposes in accordance with Wiley Terms and Conditions for Self-Archiving."en
dc.subjectEnantiopurityen
dc.subjectMetagenomic libraryen
dc.subjectStereochemistryen
dc.subjectBiocatalysten
dc.subjectEsteraseen
dc.titleIdentification of an esterase isolated using metagenomic technology which displays an unusual substrate scope and its characterisation as an enantioselective biocatalysten
dc.typeArticle (peer-reviewed)en
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