Synthesis and properties of lignin peroxidase from Streptomyces viridosporus T7A.
The production of lignin peroxidase by Streptomyces 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 degrees C, 6, and 3 mM, respectively. Stability of lignin peroxidase was determined at 37, 45, and 60 degrees C, and over the pH range 4-9.
Department of Chemical Engineering, University of Idaho, Moscow 83843.
S J
SJ
Loudha
R A
RA
Korus
D L
DL
Crawford
D004794:Enzyme Repression; D005285:Fermentation; D005947:Glucose / Q000494:pharmacology; D007700:Kinetics; D008433:Mathematics; D008962:Models, Theoretical; D010544:Peroxidases / Q000096:biosynthesis / Q000378:metabolism*; D013302:Streptomyces / Q000201:enzymology* / Q000254:growth & development
D010544:Peroxidases; C042858:lignin peroxidase; D005947:Glucose