Some characteristics and partial purification of the Ganoderma lucidum cellulase system.
The extracellular cellulase system of the white-rotting basidiomycete Ganoderma lucidum was characterised while growing in cellulose-containing shaken liquid culture. The protein content of the culture filtrate reached its maximum after 36 days and cellulase activity at about 60 days. Different cellulase activities (endoglucanase, cellobiohydrolase and beta-glucosidase) were determined in a range of pH extending from 6 to 2. All of the three enzyme activities have at least three peaks between pH 6 and 2, although optimum points of the different enzymes are slightly different, showing that the enzyme complex consists of a number of enzymes and isozymes. Partial purification of the enzyme complex was carried out by DEAE-cellulose column chromatography. Using 0-3 M linear urea gradient, protein was eluted in one sharp peak corresponding mainly to beta-glucosidase activity. Comparing crude extracellular protein with that of purified by the column using PAGE indicated that this method was suitable for the separation and partial purification of one type of Ganoderma cellulases.
Jakucs
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Department of Plant Anatomy, Eötvös Loránd University, Budapest.
Rácz
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I
Lásztity
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D001487:Basidiomycota / Q000201:enzymology*; D002480:Cellulase / Q000302:isolation & purification*; D002848:Chromatography, DEAE-Cellulose
D002480:Cellulase