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Identification of an esterase isolated using metagenomic technology which displays an unusual substrate scope and its characterisation as an enantioselective biocatalyst
Gavin, Declan P.
Murphy, Edel J.
Foley, Aoife M.
Castilla, Ignacio Abreu
Reen, F. Jerry
Woods, David F.
Collins, Stuart G.
Maguire, Anita R.
Evaluation 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.
Enantiopurity , Metagenomic library , Stereochemistry , Biocatalyst , Esterase
Gavin, 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.201801691
© 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."