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Ligninolytic enzymes of the white-rot fungus Phlebia radiata

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Niku-Paavola, M L, Karhunen, E, Salola, P, Raunio, V·1988·Biochemical Journal

Abstract

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.

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Metadata

Authors
Niku-Paavola, M. L., Karhunen, E., Salola, P., & Raunio, V
Venue
Biochemical Journal
Published
1988-09-15
Volume
254
Issue
3
Pages
877-884
ISSN
  • 0264-6021 (ISSN-L)
  • 1470-8728
OpenAlex
W1920665771
Cited by
446
References
0
FWCI
19.94
Type
journal article
Language
en
Open access
bronze

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CoChat. (2026). Citation check: Ligninolytic enzymes of the white-rot fungus Phlebia radiata. https://app.cochat.ai/papers/10.1042/bj2540877
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Niku-Paavola, M. L., Karhunen, E., Salola, P., & Raunio, V. (1988). Ligninolytic enzymes of the white-rot fungus Phlebia radiata. Biochemical Journal. https://doi.org/10.1042/bj2540877

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