Synthesis and properties of lignin peroxidase fromstreptomyces viridosporus T7A
- 89 Downloads
The production of lignin peroxidase byStreptomyces viridosporus T7A was studied in shake flasks and under aerobic conditions in a 7.5-L batch fermentor. Lignin peroxidase synthesis was found to be strongly affected by catabolite repression. Lignin peroxidase was a non-growth-associated, secondary metabolite. The maximum lignin peroxidase activity was 0.064 U/mL at 36 h.
In order to maximize lignin peroxidase activity, optimal conditions were determined. The optimal incubation temperature, pH, and substrate (2,4-dichlorophenol) concentration for the enzyme assays were 45°C, 6, and 3 mM, respectively. Stability of lignin peroxidase was determined at 37, 45, and 60°C, and over the pH range 4–9.
Index EntriesLignin peroxidase Streptomyces viridosporus enzyme synthesis
Unable to display preview. Download preview PDF.
- 2.Pridham, T. G., and Gottlieb, D. (1948),J. Microbiol. 56, 107–114.Google Scholar
- 3.Pasti, M. B., Pometto, A. L. III, Nuti, M. P., and Crawford, D. L. (1990),Appl. Environ. Microbiol. 56, 2213–2118.Google Scholar
- 5.Ramachandra, M., Adhi, T. P., and Crawford, D. L., The influence of culture parameters on the production of lignin peroxidase byStreptomyces viridosporous T7A. Poster presented at ASM Annual Meeting, New Orleans, May (1989).Google Scholar
- 7.Faison, B. D., and Kirk, T. K. (1985),Appl. Environ. Microbiol. 49, 299–304.Google Scholar