Article
Kinetic studies of Gly28:Ser mutant form of Bacillus pumilus lipase: changes in k(cat) and thermal dependence.
Biochimica et biophysica acta - 1 Dec 2010
Bustos-Jaimes Ismael, Mora-Lugo Rodrigo, Calcagno Mario L, Farrés Amelia
Abstract excerpt
Lipases are useful catalysts for a wide variety of industrial purposes. Herein we report the stability and thermal dependence of the activity of wild-type Bacillus pumilus lipase (BplA) and four site-directed mutants designed to improve its thermal stability. The Gly28:Ser mutation produces a dramatic four-fold increase in its k(cat) and a remarkable increase in its stability. While the increase in k(cat) is...
Topics
- Algorithms
- Amino Acid Sequence
- Amino Acid Substitution
- Bacillus
- Bacterial Proteins
- Biocatalysis
- Cloning, Molecular
- DNA, Bacterial
- Enzyme Stability
- Glycine
- Kinetics