Identification of an Esterase Isolated Using Metagenomic Technology which Displays an Unusual Substrate Scope and its Characterisation as an Enantioselective Biocatalyst

Citation:
Gavin DP, Murphy EJ, Foley AM, Castilla IA, Reen FJ, Woods DF, Collins SG, O'Gara F, Maguire AR. Identification of an Esterase Isolated Using Metagenomic Technology which Displays an Unusual Substrate Scope and its Characterisation as an Enantioselective Biocatalyst. Advanced Synthesis and Catalysis. 2019;361(11):2466-74

Keywords:
Biocatalyst; Enantiopurity; Esterase; Metagenomic Library; Stereochemistry

Abstract:
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 (e.g. methyl group) at the β-carbon.