The β-glucosidase of a root parasitic angiosperm, Orobanche minor Sm., was purified and characterized. The optimum pH and temperature for activity of the enzyme were 5.0 and 50 °C. The β-glucosidase was stable at up to 50 °C at pH 4.0–10.0. The Mr was estimated to be 33 kD by SDS–PAGE. The enzyme hydrolyzed p-nitrophenyl-β-D-glucopyranoside and salicin, but not the cell wall of O. minor or cellohexaose.
