ArticleInternational journal of molecular sciences2010
Expression of an organic solvent stable lipase from Staphylococcus epidermidis AT2.
Article in International journal of molecular sciences, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 19 citations in OpenAlex.
- The Role of Surface Exposed Lysine in Conformational Stability and Functional Properties of Lipase fromMolecules (Basel, Switzerland) · 2020Article
- Insight into Improved Thermostability of Cold-Adapted Staphylococcal Lipase by Glycine to Cysteine Mutation.Molecules (Basel, Switzerland) · 2019Article
- Directed Evolution of Recombinant C-Terminal Truncated Staphylococcus epidermidis Lipase AT2 for the Enhancement of Thermostability.International journal of molecular sciences · 2017Article
- Identification, characterization, and immobilization of an organic solvent-stable alkaline hydrolase (PA27) from Pseudomonas aeruginosa MH38.Molecules (Basel, Switzerland) · 2014Article
- Unscrambling the effect of C-terminal tail deletion on the stability of a cold-adapted, organic solvent stable lipase from Staphylococcus epidermidis AT2.Molecular biotechnology · 2014Article
- A new cold-adapted, organic solvent stable lipase from mesophilic Staphylococcus epidermidis AT2.The protein journal · 2014Article
- Expression and purification of organic solvent stable lipase from soil metagenomic library.World journal of microbiology & biotechnology · 2012Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
An organic solvent tolerant lipase gene from Staphylococcus epidermidis AT2 was successfully cloned and expressed with pTrcHis2 in E. coli TOP10. Sequence analysis revealed an open reading frame (ORF) of 1,933 bp in length which coded for a polypeptide of 643 amino acid residues. The polypeptide comprised of a signal peptide (37 amino acids), pro-peptide and a mature protein of 390 amino acids. Expression of AT2 lipase resulted in an 18-fold increase in activity, upon the induction of 0.6 mM IPTG after a 10 h incubation period. Interestingly, this lipase was stable in various organic solvents (25% (v/v), mainly toluene, octanol, p-xylene and n-hexane). Literature shows that most of the organic solvent stable bacterial lipases were produced by Pseudomonas sp. and Bacillus sp., but very few from Staphylococcus sp. This lipase demonstrates great potential to be employed in various industrial applications.
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