Abstract
A species of the imperfect fungus Monilia produced cellobiose dehydrogenase extracellularly when grown on cellulose. The inducible enzyme was both bound to the mycelium and released into the growth medium. The enzyme showed a high degree of specificity for cellobiose, but also oxidized lactose and 4-β-glucosylmannose. The specificity of the electron acceptor was restricted to those compounds having a redox potential of +0·22 V. p-Benzoquinone and several other quinones, however, were not reduced. Oxygen was not consumed nor was hydrogen peroxide produced by cellobiose dehydrogenase oxidation of cellobiose. The enzyme had a molecular weight of 48000 and an isoelectric point of 5·3 to 5·5. A new zymogram technique was developed for the detection of cellobiose dehydrogenase in polyacrylamide gels following electrophoresis and isoelectric focusing.
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