Topic
Esterase
About: Esterase is a research topic. Over the lifetime, 7622 publications have been published within this topic receiving 168270 citations.
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TL;DR: The esterase acted in synergism with other xylanolytic enzymes, which was reflected in increased production of phenolic acids from wheat straw xylo-oligosaccharides in the presence of xylanases of Trichoderma reesei.
148 citations
TL;DR: The electrophoretic profiles of esterase activity in protein extracts from coumaphos and permethrin-resistant strains compared to the susceptible strain revealed distinct differences, which inhibitor studies attributed to carboxylesterases.
148 citations
TL;DR: The Escherichia coli ferric enterobactin esterase gene (fes) was cloned into the vector pGEM3Z under the control of the T7 gene 10 promoter and overexpressed to approximately 15% of the total cellular protein, exhibiting a 4-fold greater activity on the free ligand.
147 citations
TL;DR: It is proposed that hydrolases in saliva increase the wear rate of composite resin fillings as well as the rate constants of the enzymatic hydrolysis of various (di)methacrylates.
Abstract: Di- and monomethacrylates hydrolyze to methacrylic acid and the alcohol part at neutral pH catalyzed by an unspecific esterase (hydrolase) and by enzymes in saliva. The rate constants of the enzymatic hydrolysis of various (di)methacrylates increase in the following order: HPMA less than BISGMA less than LAMA less than DECMA less than TEGDMA less than UEDMA less than DEGDMA. Esterase added to aqueous slurries of various powders made of polymerized BISGMA/TEGDMA-mixtures gave rise to liberation of methacrylic acid, presumably deriving from degradation of those of the dimethacrylates only bonded in the matrix by one end of the molecule. It was estimated that a TEGDMA-polymer will be hydrolyzed faster than a BISGMA-polymer. It is proposed that hydrolases in saliva increase the wear rate of composite resin fillings.
147 citations
TL;DR: Functional proteomics was used to detect non-HSL lipase(s) in mouse WAT and discovered two peaks of esterase activity using p-nitrophenyl butyrate as a substrate, which contained most of the lipase activity.
147 citations