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

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. isopropyl 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.

Biodegradable Polymer Theranostic Fluorescent Nanoprobe for Direct Visualization and Quantitative Determination of Antimicrobial Activity

“…Aliphatic esters are very well known to undergo enzymatic-biodegradation by the intracellular enzymes such as esterase enzymes in mammalian cells and bacterial lipase enzyme. The ester linkages in lipid molecules are readily hydrolyzed by esterase and lipase enzymes, depending on the short or long aliphatic chains, respectively . Recent studies also supported the presence of esterase and lipase enzymes in significant amounts in Gram-negative bacteria E.…”

“…The ester linkages in lipid molecules are readily hydrolyzed by esterase and lipase enzymes, depending on the short or long aliphatic chains, respectively. 67 Recent studies also supported the presence of esterase and lipase enzymes in significant amounts in Gram-negative bacteria E. coli to be responsible for the catalytic activity of ester hydrolysis in lipids. 68−70 Further, few reports recently reported the usage of lipase in the biodegradation of PCL chains.…”

Identification and expression of MarCE, a marine carboxylesterase with synthetic ester‐degrading activity

“…Although marine ecosystems have become increasingly valued as a source of microbial biocatalysts, marine microorganisms and their enzymes are still relatively underutilized from a biotechnological standpoint, particularly when compared to their terrestrial counterparts (Rotter et al., 2021 ). Nonetheless, efforts to characterize marine microbial activities have to date proven worthwhile, leading to an increased diversity in the pool of available biocatalysts and the identification of enzymes with novel properties including high salt tolerance, temperature adaptivity, barophilicity and unique substrate specificities (Gavin et al., 2019 ; Rodrigues et al., 2017 ; Trincone, 2017 ). In particular, microbial enzymes produced by microorganisms isolated from marine sponges are rarely reported on, but represent a potentially promising biodiscovery resource, especially considering the important role they play in the degradation of organic matter that is extracted by the sponge from the large quantities of seawater being pumped through its filter‐feeding structures for energy and nutrient gain (de Oliveira et al., 2020 ; Wang, 2006 ).…”