Activity and specificity studies of the new thermostable esterase EstDZ2

[Display omitted] •Activity and specificity of the new thermostable carboxyl esterase EstDZ2 was studied extensively for the first time.•EstDZ2 is an extremely active enzyme in the hydrolysis of aryl-substituted medium chain carboxylates.•EstDZ2 was tested for the first time in the kinetic resolutio...

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Bibliographic Details
Published in:Bioorganic chemistry 2020-11, Vol.104, p.104214, Article 104214
Main Authors: Myrtollari, Kamela, Katsoulakis, Nikolaos, Zarafeta, Dimitra, Pavlidis, Ioannis V., Skretas, Georgios, Smonou, Ioulia
Format: Article
Language:English
Subjects:
Alcohols - chemistry
Alcohols - metabolism
Biocatalysis
Butyric Acid - chemistry
Butyric Acid - metabolism
Esterases - chemistry
Esterases - isolation & purification
Esterases - metabolism
Gene Library
Hot Springs
Hydrolysis
In-silico analysis
Kinetic resolution
Molecular Docking Simulation
Molecular Structure
Temperature
Thermostable esterase
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Summary:[Display omitted] •Activity and specificity of the new thermostable carboxyl esterase EstDZ2 was studied extensively for the first time.•EstDZ2 is an extremely active enzyme in the hydrolysis of aryl-substituted medium chain carboxylates.•EstDZ2 was tested for the first time in the kinetic resolution of secondary alcohols and showed (R) enantioselectivity.•Docking experiments revealed activity and stereoselectivity profile of EstDZ2. 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.
ISSN:0045-2068
1090-2120
DOI:10.1016/j.bioorg.2020.104214