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Title: 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 m-M, respectively. Stability of lignin peroxidase was determined at 37, 45, and 60{degrees}C, and over the pH range 4-9.
Authors:
; ;  [1]
  1. Univ. of Idaho, Moscow, ID (United States)
Publication Date:
OSTI Identifier:
431598
Report Number(s):
CONF-900512-
TRN: 96:006510-0038
Resource Type:
Conference
Resource Relation:
Conference: 12. symposium on biotechnology fuels and chemicals, Gatlinburg, TN (United States), 7-11 May 1990; Other Information: PBD: 1991; Related Information: Is Part Of Twelfth symposium on biotechnology for fuels and chemicals; Greenbaum, E. [ed.] [Oak Ridge National Lab., TN (United States)]; Wyman, C.E. [ed.] [Solar Energy Research Inst., Golden, CO (United States)]; PB: 934 p.
Publisher:
Humana Press, Clifton, NJ (United States)
Research Org:
Oak Ridge National Lab., TN (United States); Badger Engineers, Inc., Tampa, FL (United States); Solar Energy Research Inst., Golden, CO (United States)
Country of Publication:
United States
Language:
English
Subject:
09 BIOMASS FUELS; 55 BIOLOGY AND MEDICINE, BASIC STUDIES; LIGNIN; DEPOLYMERIZATION; PEROXIDASES; ENZYME ACTIVITY; BIOSYNTHESIS; AEROBIC CONDITIONS; BIOTECHNOLOGY; STREPTOMYCES; TEMPERATURE DEPENDENCE; PH VALUE; BIOMASS; FERMENTATION