Hyperproducing constitutive D-serine deaminase mutant E,coli were selected by a chemostat method. The specific activity of the enzyme in these mutants is 25fold higher in comparison with the fully induced parental strain.
Selection of constitutive tryptophanase hyperproducing mutants ofEscherichia coli
✍ Scribed by E. Pavlasová; E. Stejskalová; B. Sikyta
- Publisher
- Springer Netherlands
- Year
- 1983
- Tongue
- English
- Weight
- 358 KB
- Volume
- 5
- Category
- Article
- ISSN
- 0141-5492
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✦ Synopsis
Constitutive tryptophanase hyperproducing mutants of Escherichia coli were isolated. The specific enzyme activities of these mutants are 3-5 times higher than those of the fully induced wild-type strain and the enzyme synthesis is more resistant to catabolite repression.
📜 SIMILAR VOLUMES
When arsenate-resistant mutants are selected approximately 50 per cent of them are also consitutive for the synthesis of alkaline phosphatase and the Pi-binding protein. Some of these mutants are linked to ilv (phoS- or phoT-), other are linked to proC (phoR-). One of the mutant strains linked to il