Crude cell wall preparations from Cicer urietinurn L. cell suspension cultures show high activity for the hydrolysis of coniferyl alcohol P-D-glucoside (coniferin). Various 0-glucosidase activities could be solubilized from these preparations by 0.5 M NaCl treatment and one of these could be shown to possess a high activity for the hydrolysis of coniferin. The enzyme activities were purified to near homogeneity by Sephadex G-200 and CM-Sephadex chromatography. Isoelectric focussing indicated the occurrence of P-glucosidase isoenzymes with identical catalytic activity (PI 8.5 -10).Molecular weights were determined as 110000, with two subunits of 63000 and 43000. Maximum hydrolytic activity is at pH 5.The P-glucosidase isoenzymes catalyze the hydrolysis of various P-glucosides with aromatic aglycone structure and different sugar moieties. However, coniferin has been found to be one of the best substrates ( k , = 0.8 mM; V = 6 pmol . min-' . mg protein-') for these P-glucosidase isoenzymes. The data suggest that a P-glucosidase-catalyzed reaction might be involved in lignification of these plant cell cultures.

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