Title of article :
Highly soluble expression and molecular characterization of an organic solvent-stable and thermotolerant lipase originating from the metagenome
Author/Authors :
Fan، نويسنده , , Xinjiong and Liu، نويسنده , , Xiaolong and Wang، نويسنده , , Kui and Wang، نويسنده , , Sidi and Huang، نويسنده , , Rui and Liu، نويسنده , , Yuhuan، نويسنده ,
Issue Information :
روزنامه با شماره پیاپی سال 2011
Pages :
8
From page :
319
To page :
326
Abstract :
A novel organic solvent-stable and thermotolerant lipase gene (designated ostl28) was cloned from a metagenomic library and overexpressed in Escherichia coli BL21 (DE3) in soluble form. OSTL28 contained 262 amino acids with relative molecular mass 30.1 kDa and isoelectric point 9.7. The optimum pH and temperature of the OSTL28 were 7.5 and 60 °C, respectively. OSTL28 was stable in the pH range of 4.5–9.5 and at temperatures below 65 °C. The enzyme could hydrolyze a wide range of ρ-nitrophenyl esters, but its best substrate is ρ-nitrophenyl laurate with the highest activity of 236 U/mg (54,000 U/L). The recombinant OSTL28 was highly resisted to organic solvents, especially glycerol and methanol. The metal ions, with the exception of Hg2+ and Ag+, did not have any influence on enzyme activity, whereas non-ionic surfactants and Al3+ slightly activated the enzyme. These features indicate that it is a potential biocatalyst for biodiesel production.
Keywords :
Thermotolerance , organic solvent tolerance , Highly soluble expression , Lipase , Metagenomic
Journal title :
Journal of Molecular Catalysis B Enzymatic
Serial Year :
2011
Journal title :
Journal of Molecular Catalysis B Enzymatic
Record number :
1715465
Link To Document :
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