Is cellobiose dehydrogenase from Phanerochaete chrysosporium a lignin degrading enzyme?
Cellobiose dehydrogenase (CDH) is an extracellular redox enzyme of ping-pong type, i.e. it has separate oxidative and reductive half reactions. Several wood degrading fungi produce CDH, but the biological function of the enzyme is not known with certainty. It can, however, indirectly generate hydroxyl radicals by reducing Fe(3+) to Fe(2+) and O2 to H2O2. Hydroxyl radicals are then generated by a Fenton type reaction and they can react with various wood compounds, including lignin. In this work we study the effect of CDH on a non-phenolic lignin model compound (3,4-dimethoxyphenyl glycol). The results indicate that CDH can affect lignins in three important ways. (1) It breaks beta-ethers; (2) it demethoxylates aromatic structures in lignins; (3) it introduces hydroxyl groups in non-phenolic lignins. The gamma-irradiated model compound gave a similar pattern of products as the CDH treated model compound, when the samples were analyzed by HPLC, suggesting that hydroxyl radicals are the active component of the CDH system.
Henriksson
G
G
Department of Pulp and Paper Technology and Chemistry, Royal Institute of Technology, Stockholm, Sweden. ghenrik@woodchem.kth.se
Zhang
L
L
Li
J
J
Ljungquist
P
P
Reitberger
T
T
Pettersson
G
G
Johansson
G
G
D002237:Carbohydrate Dehydrogenases / Q000378:metabolism*; D002851:Chromatography, High Pressure Liquid; D008401:Gas Chromatography-Mass Spectrometry; D006868:Hydrolysis; D008031:Lignin / Q000378:metabolism*; D020075:Phanerochaete / Q000201:enzymology*
D008031:Lignin; D002237:Carbohydrate Dehydrogenases; C019859:cellobiose-quinone oxidoreductase