Article
Study of the effect of F17A mutation on characteristics of Bacillus thermocatenulatus lipase expressed in Pichia pastoris using in silico and experimental methods.
Biotechnology and applied biochemistry - 1 Jan 2000
Karimi Esmat, Karkhane Ali Asghar, Yakhchali Bagher, Shamsara Mehdi, Aminzadeh Saeed, Torktaz Ibrahim, Hosseini Mostafa, Safari Zahra
Abstract excerpt
Bacillus thermocatenulatus lipase 2 (BTL2), a thermoalkalophilic lipase, is the best studied enzyme for its particular properties, which make it useful in different industries. Displacement of conserved phenylalanine 17 (Phe-17) residue in the active site of BTL2 has a critical role in oxyanion hole formation, which is important for enzyme activity. In this study, to facilitate oxyanion hole formation, Phe-17 was...
Topics
- Bacillus
- Gene Expression
- Lipase
- Molecular Docking Simulation
- Mutation
- Phenylalanine
- Pichia
