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A novel esterase from a soil metagenomic library displaying a broad substrate range.
- Source :
-
AMB Express . 3/5/2021, Vol. 11 Issue 1, p1-10. 10p. - Publication Year :
- 2021
-
Abstract
- A novel esterase gene was isolated from a soil metagenomic library. The gene encoded a protein of 520 amino acids which contained a 21 aa signal peptide. Primary structure analysis of the protein sequence revealed that it contained a conserved active site motif (SxSxG) and a structural motif (CS-D-HC). Then the esterase gene was cloned and expressed in Escherichia coli BL21(DE3). SDS-PAGE analysis of the purified esterase showed that it was expressed in a highly soluble form and its molecular mass was estimated to be 55 kDa. Characterization of the esterase revealed that it exhibited high activity toward p-nitrophenyl esters with short acyl chains and especially p-nitrophenyl acetate, suggesting that it was a typical carboxylesterase rather than a lipase. With p-nitrophenyl acetate as substrate, the enzyme showed its optimal activity at pH 7.0 and 30 °C, and it was stable at a broad pH range from 4.5 to 10.0 and temperature not higher than 50 °C. Furthermore, the enzyme showed different substrate specificity from known esterase, it was not only hydrolyzing against p-nitrophenyl esters, but also hydrolyzing all hydroxybenzoic esters and hydroxycinnamic ester assayed. As it was an enzyme active on a broad range of phenolic esters, simultaneously possessing feruloyl esterase, chlorogenate esterase and tannase activities, it could serve as a valuable candidate for applications in biotechnology. [ABSTRACT FROM AUTHOR]
- Subjects :
- *AMINO acid sequence
*MOLECULAR weights
*MOLECULAR cloning
*GENES
*SOILS
*LIPASES
Subjects
Details
- Language :
- English
- ISSN :
- 21910855
- Volume :
- 11
- Issue :
- 1
- Database :
- Academic Search Index
- Journal :
- AMB Express
- Publication Type :
- Academic Journal
- Accession number :
- 149092065
- Full Text :
- https://doi.org/10.1186/s13568-021-01198-5