[beta-Glucosidase of leaves and roots of the common beet Beta vulgaris].
beta-Glucosidases detected in the leaves and roots of common beet, Beta vulgaris, have been demonstrated to catalyze hydrolysis of native betacyanins. A method is described for the isolation and purification of beta-glucosidase from the roots, which involves ammonium sulfate precipitation, DEAE-cellulose chromatography, and Sephadex gel filtration. Maximum activity of the enzyme is detected at 50 degrees C and pH 8.0; it retains stability within the pH range from 5.1 to 9.2. In the leaves, beta-glucosidase is chloroplast membrane-associated; solubilization of the membranes results in the enzyme inactivation.
Zakharova
N S
NS
Bach Institute of Biochemistry of the Russian Academy of Sciences, Moscow, Russia.
Petrova
T A
TA
D019663:Chenopodiaceae / Q000201:enzymology*; D002848:Chromatography, DEAE-Cellulose; D002850:Chromatography, Gel; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D018515:Plant Leaves / Q000201:enzymology*; D001617:beta-Glucosidase / Q000302:isolation & purification / Q000378:metabolism*
D001617:beta-Glucosidase