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Applied Biochemistry and Biotechnology

, Volume 28, Issue 1, pp 411–420 | Cite as

Synthesis and properties of lignin peroxidase fromstreptomyces viridosporus T7A

  • S. J. Lodha
  • R. A. Korus
  • D. L. Crawford
Session 3 Applied Biological Research II

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.

Index Entries

Lignin peroxidase Streptomyces viridosporus enzyme synthesis 

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Copyright information

© Humana Press Inc. 1991

Authors and Affiliations

  • S. J. Lodha
    • 1
  • R. A. Korus
    • 1
  • D. L. Crawford
    • 2
  1. 1.Department of Chemical EngineeringUniversity of IdahoIDMoscow
  2. 2.Department of Bacteriology and BiochemistryUniversity of IdahoIDMoscow

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