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The beta-glucosidase, beta-galactosidase, beta-xylosidase and alpha-L-arabinosidase activities of a partially purified preparation from sunflower seeds were studied by chromatography, polyacrylamide gel electrophoresis and isoelectrofocusing. beta-Glucosidase was isolated as two fractions with high molecular weights. One form of beta-glucosidase does not possess strict specificity to stereochemistry of hexosides C-4 and C-6 and pentosides C-5, whereas the second form exhibits a narrow specificity for C-4 and is low specific towards substituents of C-5. The sunflower seeds also contain acid beta-galactosidase, which possesses a narrow specificity and is not coupled with the beta-glucosidase activity. The molecular weight of beta-galactosidase is 62000.

Beta-Glucosidase, beta-galactosidase, beta-xylosidase and alpha-L-arabinosidase activities of partially purified preparation of almond emulsin were investigated using chromatography, electrophoresis in polyacrylamide gel and isoelectric focusing. Beta-Glucosidase was found to exist as two components having equal molecular weight. Aggregation of the components with inactive proteins probably results in the appearance of multiple native forms which have similar specific activities. In no case separation of the beta-glucosidase activity from the accompanied activities was achieved. It is concluded therefore that these activities are exhibited by an enzyme which is not strictly specific to the C4, C6 stereochemistry for hexosides and to that of C4, C5 for pentozides.