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Research was performed to analyze the purification and characterization of alpha-L-Arabinofuranosidase from a color-variant strain of the yeast-like fungus Aureobasidium pullulans. Results revealed that a color-variant strain of A. pullulans produced an extracellular highly thermostable alpha-L-Arabinofuranosidase, which was able to hyrolyze both 1->3 and 1->5 linkages in arabinan, when grown in liquid culture on oat spelt xylan. Evidence also suggested that the enzyme did not necessitate metal ion for activity and was not affected by p-chloromercuribenzoate and dithiothreitol.

The beta-glucosidase produced and purified from Candida peltata hydrolyzes cellobiose, shows a synergistic interaction with cellulase and has high glucose tolerance. The enzyme is a monomeric protein with a molecular weight of 43,000, and has maximum activity at 50 degrees celsius and 5.0 pH. The beta-glucosidase has little transglucosylation activity. Divalent cations are unessential for the enzymatic activity which is unaffected by p-chloromercuribenzoate.

Growth of a color variant strain of Aureobasidium pullulans in a liquid culture with various carbon sources leads to the production of an extracellular thermostable beta-glucosidase. The enzyme exhibits optimal activity at 75 degrees Celsius and pH 4.5. Methods including ammonium sulfate treatment help purify the extracellular beta-glucosidase. The purified enzyme hydrolyzes different cell oligosaccharides, and its activity is inhibited by glucose.