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Updated: Mar 9, 2026

Functional Characterization of Carboxylesterases in Insecticide Resistant House Flies, Musca Domestica
Published on: August 23, 2018
A novel, versatile family IV carboxylesterase exhibits high stability and activity in a broad pH spectrum
Amélie Dukunde1, Dominik Schneider1, Mingji Lu1
1Department of Genomic and Applied Microbiology and Göttingen Genomics Laboratory, Institute of Microbiology and Genetics, Georg-August University Göttingen, Grisebachstr. 8, 37077, Göttingen, Germany.
Objectives:
To investigate the properties of a novel metagenome-derived member of the hormone-sensitive lipase family of lipolytic enzymes.
Results:
A forest soil metagenome-derived gene encoding an esterase (Est06) belonging to the hormone-sensitive lipase family of lipolytic enzymes was subcloned, heterologously expressed and characterized. Est06 is a polypeptide of 295 amino acids with a molecular mass of 31 kDa. The deduced protein sequence shares 61% similarity with a hypothetical protein from the marine symbiont Candidatus Entotheonella sp. TSY1. Purified Est06 exhibited high affinity for acyl esters with short-chain fatty acids, and showed optimum activity with p-nitrophenyl valerate (C5). Maximum enzymatic activity was at 50 °C and pH 7. Est06 exhibited high stability at moderate temperatures by retaining all of its catalytic activity below 30 °C over 13 days. Additionally, Est06 displayed high stability between pH 5 and 9. Esterase activity was not inhibited by metal ions or detergents, although organic solvents decreased activity.
Conclusions:
The combination of Est06 properties place it among novel biocatalysts that have potential for industrial use including low temperature applications.
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