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Cloning, expression and biochemical characterization of a novel, moderately thermostable GDSL family esterase from Geobacillus thermodenitrificans T2

Paper ID Volume ID Publish Year Pages File Format Full-Text
20825 43193 2013 5 PDF Available
Title
Cloning, expression and biochemical characterization of a novel, moderately thermostable GDSL family esterase from Geobacillus thermodenitrificans T2
Abstract

A thermostable GDSL family esterase-encoding gene, EstL5, was directly obtained from the genomic DNA of Geobacillus thermodenitrificans T2. Recombinant hexahistidine-tagged EstL5 was overexpressed, purified, and its biochemical properties were partially characterized. EstL5 was observed to be active within the temperature range of 0–80°C, having maximal activity at 60°C. Unlike most other thermostable enzymes, EstL5 displayed 24% of its highest activity at 0°C. EstL5 exhibited a high level of activity within a pH range of 6.0–11.0, showing the highest activity at pH 8.0. EstL5 also retained 100% of its activity after a 12-h incubation at 55°C. Furthermore, this enzyme was observed to be strongly inhibited by 10% (w/v) SDS and 0.1 mM PMSF.

Keywords
Thermostable esterase; GDSL family; Cloning; Characterization; Geobacillus
First Page Preview
Cloning, expression and biochemical characterization of a novel, moderately thermostable GDSL family esterase from Geobacillus thermodenitrificans T2
Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Bioscience and Bioengineering - Volume 115, Issue 2, February 2013, Pages 133–137
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering