Ligninolytic enzymes of the white-rot fungus Phlebia radiata

Marja-Leena Niku-Paavola, Eija Karhunen, Päivi Salola, Veijo Raunio

Research output: Contribution to journalArticleScientificpeer-review

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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.
Original languageEnglish
Pages (from-to)877-884
JournalBiochemical Journal
Volume254
Issue number3
DOIs
Publication statusPublished - 1988
MoE publication typeA1 Journal article-refereed

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Fungi
Enzymes
Oxidoreductases
lignin peroxidase
Prosthetics
Catalase
Epitopes
Glycoproteins
Animals
Electrons
Liquids

Cite this

Niku-Paavola, M-L., Karhunen, E., Salola, P., & Raunio, V. (1988). Ligninolytic enzymes of the white-rot fungus Phlebia radiata. Biochemical Journal, 254(3), 877-884. https://doi.org/10.1042/bj2540877
Niku-Paavola, Marja-Leena ; Karhunen, Eija ; Salola, Päivi ; Raunio, Veijo. / Ligninolytic enzymes of the white-rot fungus Phlebia radiata. In: Biochemical Journal. 1988 ; Vol. 254, No. 3. pp. 877-884.
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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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Niku-Paavola, M-L, Karhunen, E, Salola, P & Raunio, V 1988, 'Ligninolytic enzymes of the white-rot fungus Phlebia radiata', Biochemical Journal, vol. 254, no. 3, pp. 877-884. https://doi.org/10.1042/bj2540877

Ligninolytic enzymes of the white-rot fungus Phlebia radiata. / Niku-Paavola, Marja-Leena; Karhunen, Eija; Salola, Päivi; Raunio, Veijo.

In: Biochemical Journal, Vol. 254, No. 3, 1988, p. 877-884.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - Ligninolytic enzymes of the white-rot fungus Phlebia radiata

AU - Niku-Paavola, Marja-Leena

AU - Karhunen, Eija

AU - Salola, Päivi

AU - Raunio, Veijo

PY - 1988

Y1 - 1988

N2 - 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.

AB - 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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Niku-Paavola M-L, Karhunen E, Salola P, Raunio V. Ligninolytic enzymes of the white-rot fungus Phlebia radiata. Biochemical Journal. 1988;254(3):877-884. https://doi.org/10.1042/bj2540877