Enhanced production of recombinant galactose oxidase fromFusarium graminearuminE. coli
✍ Scribed by Withu Choosri; Regina Paukner; Petra Wührer; Dietmar Haltrich; Christian Leitner
- Publisher
- Springer
- Year
- 2010
- Tongue
- English
- Weight
- 239 KB
- Volume
- 27
- Category
- Article
- ISSN
- 1573-0972
No coin nor oath required. For personal study only.
📜 SIMILAR VOLUMES
## Abstract Galactose oxidase (GO) displays broad primary alcohol substrate specificity and so offers potential for engineering new substrate specificity by directed evolution. Producing variant libraries of sufficient complexity ideally requires expression of functional protein in a host such as _
Genetic manipulation of the host strain, by which cell physiology could be modulated, was exploited t o enhance recombinant protein production in Escherichia coli. The effects of an inactivated stationary-phase gene (rmf or katF) on recombinant protein production in strains with two different expres