Article
Biochemical and structural characterization of two site-directed mutants of Staphylococcus xylosus lipase.
Molecular biotechnology - 1 Oct 2010
Kolling Deise Juliana, Bertoldo Jean Borges, Brod Fábio Cristiano Angonesi, Vernal Javier, Terenzi Hernán, Arisi Ana Carolina Maisonnave
Abstract excerpt
Staphylococcus xylosus AF208229 lipase was expressed in E. coli containing an histidine-tag (WT-Val). In the present work, in order to check the importance of the residue 309 in the specific activity, the amino acid side chain residue valine 309 was substituted by aspartate or lysine through site-directed mutagenesis. Both mutant lipases (MUT-Lys and MUT-Asp) were expressed in E. coli and the recombinant...
Topics
- Amino Acid Substitution
- Bacterial Proteins
- Enzyme Stability
- Escherichia coli
- Hydrogen-Ion Concentration
- Lipase
- Mutagenesis, Site-Directed
- Mutation
- Point Mutation
- Protein Structure, Secondary