Biochemistry of the oxidation of lignin by Phangerochate chrysosporium

T. Kent Kirk, Ming Tien, Brendlyn D. Faison

Research output: Contribution to journalReview article

10 Citations (Scopus)

Abstract

The objective of this research was to identify the biochemical agents responsible for the oxidative degradation of lignin by the white-rot fungus Phanerochaete chrysosporium. We examined the hypothesis that activated oxygen species are involved, and we also sought the agent in ligninolytic cultures responsible for a specific oxidative degradative reaction in substructure model compounds. Results of studies of the production of activated oxygen species by cultures, of the effect of their removal on ligninolytic activity, and of their action on substructure model compounds support a role for hydrogen peroxide (H2O2) and possibly superoxide (O2 ·-) in lignin degradation. Involvement of hydroxyl radical (·OH) or singlet oxygen (1O2) is not supported by our data. The actual biochemical agent responsible for one important oxidative C-C bond cleavage reaction in non-phenolic lignin substructure model compounds, and in lignin itself, was found to be an enzyme. The enzyme is extracellular, has a molecular weight of 42,000 daltons, is azide-sensitive, and requires H2O2 for activity.

Original languageEnglish (US)
Pages (from-to)183-199
Number of pages17
JournalBiotechnology Advances
Volume2
Issue number2
DOIs
StatePublished - Jan 1 1984

Fingerprint

Chrysosporium
Biochemistry
Lignin
Oxidation
Oxygen
Enzymes
Phanerochaete
Degradation
Singlet Oxygen
Azides
Fungi
Hydrogen peroxide
Superoxides
Hydroxyl Radical
Hydrogen Peroxide
Molecular Weight
Molecular weight
Research

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Bioengineering
  • Applied Microbiology and Biotechnology

Cite this

Kirk, T. Kent ; Tien, Ming ; Faison, Brendlyn D. / Biochemistry of the oxidation of lignin by Phangerochate chrysosporium. In: Biotechnology Advances. 1984 ; Vol. 2, No. 2. pp. 183-199.
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Biochemistry of the oxidation of lignin by Phangerochate chrysosporium. / Kirk, T. Kent; Tien, Ming; Faison, Brendlyn D.

In: Biotechnology Advances, Vol. 2, No. 2, 01.01.1984, p. 183-199.

Research output: Contribution to journalReview article

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T1 - Biochemistry of the oxidation of lignin by Phangerochate chrysosporium

AU - Kirk, T. Kent

AU - Tien, Ming

AU - Faison, Brendlyn D.

PY - 1984/1/1

Y1 - 1984/1/1

N2 - The objective of this research was to identify the biochemical agents responsible for the oxidative degradation of lignin by the white-rot fungus Phanerochaete chrysosporium. We examined the hypothesis that activated oxygen species are involved, and we also sought the agent in ligninolytic cultures responsible for a specific oxidative degradative reaction in substructure model compounds. Results of studies of the production of activated oxygen species by cultures, of the effect of their removal on ligninolytic activity, and of their action on substructure model compounds support a role for hydrogen peroxide (H2O2) and possibly superoxide (O2 ·-) in lignin degradation. Involvement of hydroxyl radical (·OH) or singlet oxygen (1O2) is not supported by our data. The actual biochemical agent responsible for one important oxidative C-C bond cleavage reaction in non-phenolic lignin substructure model compounds, and in lignin itself, was found to be an enzyme. The enzyme is extracellular, has a molecular weight of 42,000 daltons, is azide-sensitive, and requires H2O2 for activity.

AB - The objective of this research was to identify the biochemical agents responsible for the oxidative degradation of lignin by the white-rot fungus Phanerochaete chrysosporium. We examined the hypothesis that activated oxygen species are involved, and we also sought the agent in ligninolytic cultures responsible for a specific oxidative degradative reaction in substructure model compounds. Results of studies of the production of activated oxygen species by cultures, of the effect of their removal on ligninolytic activity, and of their action on substructure model compounds support a role for hydrogen peroxide (H2O2) and possibly superoxide (O2 ·-) in lignin degradation. Involvement of hydroxyl radical (·OH) or singlet oxygen (1O2) is not supported by our data. The actual biochemical agent responsible for one important oxidative C-C bond cleavage reaction in non-phenolic lignin substructure model compounds, and in lignin itself, was found to be an enzyme. The enzyme is extracellular, has a molecular weight of 42,000 daltons, is azide-sensitive, and requires H2O2 for activity.

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