Affiliation:
1. Institute of Biotechnology, ETH-Zürich, Switzerland.
Abstract
An intracellular peroxidase (EC 1.11.1.7) from Streptomyces cyaneus was purified to homogeneity. The enzyme had a molecular weight of 185,000 and was composed of two subunits of equal size. It had an isoelectric point of 6.1. The enzyme had a peroxidase activity toward o-dianisidine with a Km of 17.8 microM and a pH optimum of 5.0. It also showed catalase activity with a Km of 2.07 mM H2O2 and a pH optimum of 8.0. The purified enzyme did not catalyze C alpha-C beta bond cleavage of 1,3-dihydroxy-2-(2-methoxyphenoxy)-1-(4-ethoxy-3-methoxyphenyl) propane, a nonphenolic dimeric lignin model compound. The spectrum of the peroxidase showed a soret band at 405 nm, which disappeared after reduction with sodium dithionite, indicating that the enzyme is a hemoprotein. Testing the effects of various inhibitors on the enzyme activity showed that it is a bifunctional enzyme having catalase and peroxidase activities.
Publisher
American Society for Microbiology
Subject
Ecology,Applied Microbiology and Biotechnology,Food Science,Biotechnology
Reference30 articles.
1. Production of major extracellular enzymes during lignocellulose degradation by two streptomycetes in agitated submerged culture;Adhi T. P.;Appl. Environ. Microbiol.,1989
2. A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding;Bradford M. M.;Anal. Biochem.,1976
3. Purification of the o-dianisidine peroxidase from E. coli B;Claiborne A.;J. Biol. Chem.,1979
4. Decker L. A. 1977. Peroxidase p. 66. In Worthington enzyme manual. Worthington Biochemical Co. Freehold N.J.
5. The potential use of ozone and peroxidase for removal of aromatic compounds from water by polymerization. Ozone Sci;Duguet J. B.;Eng.,1986
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