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- W2056548063 abstract "The cellobiose dehydrogenase secreted by Coniophora puteana (Schum ex Fr) Karsten during growth on cellulose was isolated by successive anion-exchange chromatography on Q Sepharose fast flow and on TSK DEAE-650S and gel filtration on Superose 12. The enzyme was recovered at a 41% yield with a 43-fold increase in specific activity. The purified sample was homogeneous by polyacrylamide gel electrophoresis (PAGE), sodium lauryl sulfate (SDS)-PAGE, and electrophoretic titration curve analysis and stained positively for glycoprotein (periodic acid/Schiff base reaction) and hemoprotein (peroxidase reaction). By isoelectric focusing over a narrow pH range two distinct bands were observed: a major band (pI 3.9) flanked by a minor band on its acidic side. FPLC gel filtration on TSK G3000 SW revealed a M(r) of 192,000, whereas on SDS-PAGE a single band, corresponding to a M(r) of 111,000, was observed. The enzyme contained 13% sugar as mannose and upon digestion with endoglycosidase H, its molecular weight was lowered by 11 kDa. The enzyme showed a visible spectrum compatible with that of a b-type cytochrome containing a flavin cofactor. It was able to oxidize cellobiose, cellodextrins, and lactose at their C1-reducing group, with dichlorophenol indophenol as oxidant. Oxygen consumption (oxidase reaction in a Clark electrode) was not at a detectable rate. Km and Vmax for cellobiose oxidation were 84 microM and 2.98 mumol mg-1 min-1, respectively, but the enzyme was strongly substrate (cellobiose) inhibited (Kis 5.4 mM)." @default.
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- W2056548063 date "1993-02-01" @default.
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- W2056548063 title "Isolation and Characterization of the Cellobiose Dehydrogenase from the Brown-Rot Fungus Coniophora puteana (Schum ex Fr.) Karst." @default.
- W2056548063 doi "https://doi.org/10.1006/abbi.1993.1077" @default.
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