Abstract
Cellulase in Penicillium purpurogenum strain P-26 was induced with the cellobiose-octaacetate (COA) hydrolyzate due to the crude extracellular acetyl esterase of this fungus. Of the multiple constituents of the hydrolyzate, three predominant ones were purified by silica gel chromatography. They were identified as tri-, di-, and mono- O-acetyl cellobioses with a deacetylated reducing end by mass spectrometry and 500 MHz 1H-NMR. These acetyl cellobioses apparently induced cellulase due to their slow consumption, while reference sugars such as glucose or cellobiose did not. In particular, mono- O-acetyl cellobiose was the most effective for cellulase induction among the compounds.
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