Summary: An extracellular cellobiose dehydrogenase has been purified from the culture filtrates of The purified enzyme is homogeneous as determined by disc gel electrophoresis, with and without SDS, and by analytical isoelectric focusing in polyacrylamide gel. The enzyme is a single-subunit glycoprotein containing 8·9% total carbohydrate; its is 63000-64500, and its isoelectric point 5·18. The enzyme oxidized cellobiose, other cellodextrins and lactose whereas other disaccharides tested were not utilized as substrates. The rate of cellodextrin oxidation decreased and the increased with increasing degree of polymerization of the substrate. Cytochrome was reduced though at a considerably lower rate than 2,6-dichlorophenolindophenol. The natural electron acceptor for the enzyme has not been identified.


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