Abstract
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.
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Lodha, S.J., Korus, R.A. & Crawford, D.L. Synthesis and properties of lignin peroxidase fromstreptomyces viridosporus T7A. Appl Biochem Biotechnol 28, 411–420 (1991). https://doi.org/10.1007/BF02922621
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DOI: https://doi.org/10.1007/BF02922621