P. Ander et L. Marzullo, SUGAR OXIDOREDUCTASES AND VERATRYL ALCOHOL OXIDASE AS RELATED TO LIGNIN DEGRADATION, Journal of biotechnology, 53(2-3), 1997, pp. 115-131
Properties of cellobiose:quinone oxidoreductase (CBQ), cellobiose dehy
drogenase (CDH), glyoxal oxidase (GLOX), glucose oxidases and veratryl
alcohol oxidase (VAO) are reviewed. There is strong evidence that CDH
reduces quinones, phenoxy and cation radicals. Glucose oxidases (gluc
ose 1-oxidase and pyranose 2-oxidase) and VAO have been less investiga
ted but evidence for reduction of the above compounds is accumulating.
Pyranose oxidase, glyoxal oxidase and VAO are very important for hydr
ogen peroxide production by white-rot fungi. CDH is only produced on c
ellulose or on wood, whereas pyranose oxidase and VAO are produced bot
h on wood and on rich glucose media suggesting that the lignin degradi
ng white-rot fungi may use different quinone and radical reducing enzy
mes to regulate lignin polymerization/depolymerization depending on th
e substrate and cultivation conditions. Intracellular quinone reductas
es are also produced. Whether brown-rot fungi in general produce CBQ/C
DH or VAO is not clear. The Fe(III) reducing ability of both CDH and c
ertain phenolate compounds agree with the rapid depolymerization of ce
llulose by brown-rot fungi. The interaction of Fe(III) reduction with
the hydrogen peroxide producing system in white-rot and brown-rot fung
i requires more investigation. (C) 1997 Elsevier Science B.V.