Activity and specificity studies of the new thermostable esterase EstDZ2

Kamela Myrtollari; Nikolaos Katsoulakis; Dimitra Zarafeta; Ioannis V Pavlidis; Georgios Skretas; Ioulia Smonou

doi:10.1016/j.bioorg.2020.104214

Activity and specificity studies of the new thermostable esterase EstDZ2

Bioorg Chem. 2020 Nov:104:104214. doi: 10.1016/j.bioorg.2020.104214. Epub 2020 Aug 29.

Authors

Kamela Myrtollari¹, Nikolaos Katsoulakis¹, Dimitra Zarafeta², Ioannis V Pavlidis¹, Georgios Skretas², Ioulia Smonou³

Affiliations

¹ Department of Chemistry, University of Crete, University Campus-Voutes, 70013 Heraklion, Crete, Greece.
² Institute of Chemical Biology, National Hellenic Research Foundation, 11635 Athens, Greece.
³ Department of Chemistry, University of Crete, University Campus-Voutes, 70013 Heraklion, Crete, Greece. Electronic address: smonou@uoc.gr.

PMID: 32927128
DOI: 10.1016/j.bioorg.2020.104214

Abstract

In this paper, we study the activity and specificity of EstDZ2, a new thermostable carboxyl esterase of unknown function, which was isolated from a metagenome library from a Russian hot spring. The biocatalytic reaction employing EstDZ2 proved to be an efficient method for the hydrolysis of aryl p-, o- or m-substituted esters of butyric acid and esters of secondary alcohols. Docking studies revealed structural features of the enzyme that led to activity differences among the different substrates.

Keywords: Hydrolysis; In-silico analysis; Kinetic resolution; Thermostable esterase.

MeSH terms

Alcohols / chemistry
Alcohols / metabolism
Biocatalysis
Butyric Acid / chemistry
Butyric Acid / metabolism
Esterases / chemistry
Esterases / isolation & purification
Esterases / metabolism*
Gene Library
Hot Springs
Hydrolysis
Molecular Docking Simulation
Molecular Structure
Temperature*

Substances

Alcohols
Butyric Acid
Esterases