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- W2068263022 abstract "Crude cell wall preparations from Cicer arietinum L. cell suspension cultures show high activity for the hydrolysis of coniferyl alcohol beta-D-glucoside (coniferin). Various beta-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 beta-glucosidase isoenzymes with identical catalytic activity (pI 8.5-10). Molecular weights were determined as 110 000, with two subunits of 63 000 and 43 000. Maximum hydrolytic activity is at pH 5. The beta-glucosidase isoenzymes catalyze the hydrolysis of various beta-glucosides with aromatic aglycone structure and different sugar moieties. However, coniferin has been found to be one of the best substrates (km = 0.8 mM; V = 6 mumol.min-1.mg protein-1) for these beta-glucosidase isoenzymes. The data suggest that beta-glucosidase-catalyzed reaction might be involved in lignification of these plant cell cultures." @default.
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- W2068263022 date "1978-03-01" @default.
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- W2068263022 title "Characterization of beta-Glucosidase Isoenzymes Possibly Involved in Lignification from Chick Pea (Cicer arietinum L.) Cell Suspension Cultures" @default.
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- W2068263022 doi "https://doi.org/10.1111/j.1432-1033.1978.tb12190.x" @default.
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