Article
Production of L-tryptophan from D,L-5-indolylmethylhydantoin by resting cells of a mutant of Arthrobacter species (DSM 3747).
Journal of biotechnology - 1 Jun 1990
Gross C, Syldatk C, Mackowiak V, Wagner F
Abstract excerpt
The reaction parameters and the stereospecificity of the enzymatic cleavage of D,L-5-indolylmethylhydantoin in producing L-tryptophan with resting cells of Arthrobacter sp. DSM 3747 were studied. When intact cells were tested, the optimal pH was between 8.5 and 9.0 and the optimal temperature was 50 degrees C. Both, L-N-carbamoylase and hydantoinase could be stabilized over 24 h at 30 and 40 degrees C by the...
Topics
- Amidohydrolases
- Arthrobacter
- Cell Membrane Permeability
- Deoxycholic Acid
- Enzyme Stability
- Hydantoins
- Hydrogen-Ion Concentration
- Mutation
- Stereoisomerism
- Temperature
- Tryptophan