RT Journal Article SR Electronic(1) A1 Sadana, Jai C. A1 Patil, Rajkumar V.YR 1985 T1 The Purification and Properties of Cellobiose Dehydrogenase from Sclerotium rolfsii and its Role in Cellulolysis JF Microbiology, VO 131 IS 8 SP 1917 OP 1923 DO https://doi.org/10.1099/00221287-131-8-1917 PB Microbiology Society, SN 1465-2080, AB Summary: An extracellular cellobiose dehydrogenase has been purified from the culture filtrates of Sclerotium rolfsii. 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 M r 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 K m increased with increasing degree of polymerization of the substrate. Cytochrome c was reduced though at a considerably lower rate than 2,6-dichlorophenolindophenol. The natural electron acceptor for the enzyme has not been identified., UL https://www.microbiologyresearch.org/content/journal/micro/10.1099/00221287-131-8-1917