Purification and characterization of a beta-glucosidase from the root parasitic plant Orobanche minor Sm.
The beta-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 degrees C. The beta-glucosidase was stable at up to 50 degrees C at pH 4.0-10.0. The M(r) was estimated to be 33 kD by SDS-PAGE. The enzyme hydrolyzed p-nitrophenyl-beta-D-glucopyranoside and salicin, but not the cell wall of O. minor or cellohexaose.
Sasanuma
Izumi
I
Oyama National College of Technology, Oyama, Japan. sasaki@oyama-ct.ac.jp
Hirakawa
Go
G
D001592:Benzyl Alcohols / Q000378:metabolism; D002473:Cell Wall / Q000378:metabolism; D005960:Glucosides / Q000378:metabolism; D007700:Kinetics; D009844:Oligosaccharides / Q000378:metabolism; D031672:Orobanche / Q000201:enzymology*; D013379:Substrate Specificity; D001617:beta-Glucosidase / Q000737:chemistry / Q000302:isolation & purification*
D001592:Benzyl Alcohols; D005960:Glucosides; D009844:Oligosaccharides; C099423:cellohexaose; C025193:4-nitrophenyl beta-D-glucoside; C005696:salicin; D001617:beta-Glucosidase