Article
Site-directed mutagenesis of GH10 xylanase A from Penicillium canescens for determining factors affecting the enzyme thermostability.
International journal of biological macromolecules - 1 Nov 2017
Denisenko Yury A, Gusakov Alexander V, Rozhkova Aleksandra M, Osipov Dmitry O, Zorov Ivan N, Matys Veronika Yu, Uporov Igor V, Sinitsyn Arkady P
Abstract excerpt
In order to investigate factors affecting the thermostability of GH10 xylanase A from Penicillium canescens (PcXylA) and to obtain its more stable variant, the wild-type (wt) enzyme and its mutant forms, carrying single amino acid substitutions, were cloned and expressed in Penicillium verruculosum B1-537 (niaD-) auxotrophic strain under the control of the cbh1 gene promoter. The recombinant PcXylA-wt and I6V,...
Topics
- Amino Acid Sequence
- Endo-1,4-beta Xylanases
- Enzyme Stability
- Models, Molecular
- Mutagenesis, Site-Directed
- Mutation
- Penicillium
- Protein Conformation
- Temperature