ArticleWorld journal of microbiology & biotechnology2012
Expression and purification of organic solvent stable lipase from soil metagenomic library.
Article in World journal of microbiology & biotechnology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Gene cloning, heterologous expression, and partial characterization of a novel cold-adapted subfamily I.3 lipase from Pseudomonas fluorescence KE38.Scientific reports · 2020Article
- First co-expression of a lipase and its specific foldase obtained by metagenomics.Microbial cell factories · 2014Article
- Protein engineering by random mutagenesis and structure-guided consensus of Geobacillus stearothermophilus Lipase T6 for enhanced stability in methanol.Applied and environmental microbiology · 2014Article
- Cloning and molecular modelling of pectin degrading glycosyl hydrolase of family 28 from soil metagenomic library.Molecular biology reports · 2014Article
- Cloning and characterization of newly isolated lipase from Enterobacter sp. Bn12.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2014Article
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Authors and funding
2 authors.
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Abstract
Gene for organic solvent stable lipase was overexpressed from soil metagenomic library. The clone with maximum activity was selected, and enzyme was purified by gel-permeation chromatography with a molecular mass of approx. 40 kDa. The deduced aminoacid sequence indicated that the protein belongs to the lipase family I.3 and containing a C-terminal secretion signal for ABC dependent transport together with possible motifs for Ca(2+) binding sites. The enzyme expressed maximum activity at 30 °C and pH 7.0 and found to be stable in pH and temperature ranging from 6.0-9.0 and 20-60 °C, respectively. Furthermore, the enzyme was found highly resistant to many organic solvents, especially isopropanol, DMSO, methanol, xylene and hexane. The enzyme showed enhanced activity in the presence of divalent cations (Mg(2+), Mn(2+), Ca(2+), Hg(2+), Cu(2+)), whereas the presence of trivalent cation (Fe(3+)) inhibited the activity.
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