Ligninolytic enzymes of the white-rot fungus Phlebia radiata

One oxidase (EC 1.10.3.2) and three lignin peroxidases (EC 1.11.1.-) were purified from the culture liquid of the white-rot fungus Phlebia radiata Fr. All the enzymes were glycoproteins. The oxidase had Mr 64,000 and the lignin peroxidases I, II and III had Mr values 42,000, 45,000 and 44,000 respec...

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Bibliographic Details
Published in:Biochemical journal 1988-09, Vol.254 (3), p.877-884
Main Authors: Niku-Paavola, M L, Karhunen, E, Salola, P, Raunio, V
Format: Article
Language:English
Subjects:
Benzyl Alcohols - metabolism
Carbohydrates
Chromatography, High Pressure Liquid
Fungi - enzymology
Hydrogen Peroxide
Immunoelectrophoresis
Laccase
Lignin - metabolism
Oxidoreductases - isolation & purification
Oxidoreductases - metabolism
Peroxidases - isolation & purification
Peroxidases - metabolism
Spectrophotometry
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Summary:One oxidase (EC 1.10.3.2) and three lignin peroxidases (EC 1.11.1.-) were purified from the culture liquid of the white-rot fungus Phlebia radiata Fr. All the enzymes were glycoproteins. The oxidase had Mr 64,000 and the lignin peroxidases I, II and III had Mr values 42,000, 45,000 and 44,000 respectively. The lignin peroxidases were found to share common antigenic determinants: lignin peroxidases II and III were serologically indistinguishable and lignin peroxidase I was related but distinguishable. The oxidase did not share any immunological properties with the lignin peroxidases. Lignin peroxidases of Phlebia contain protoporphyrin IX as a prosthetic group. In the presence of H2O2 and an electron donor, veratryl alcohol, lignin peroxidases exhibit spectral shifts analogous to those of animal catalase (EC 1.11.1.6). Phlebia enzymes show optimal activity at pH 3-4.5 at 40 degrees C and are stable in the pH range 5-6. They modify Kraft lignin and phenolic compounds containing hydroxy and methoxy groups.
ISSN:0264-6021
1470-8728
DOI:10.1042/bj2540877