Cationic form of beta-galactosidase in the germinating seeds of Vigna sinensis (Linn) Savi.
The cationic form of beta-galactosidase (EC 3.2.1.23) from the germinating seeds of Vigna sinensis has been separated from its other isoforms by DEAE-cellulose (DE-52) column chromatography and further purified by gel filtration and affinity chromatography. Polyacrylamide gel electrophoresis of the purified enzyme imparted a single protein band. The molecular mass of the enzyme as determined by Sephadex G-150 gel filtration is 58,800 Da. The optimum temperature and the optimum pH are 60 degrees C and 4.5, respectively. Most of the metal ions tested were inhibitory to the enzyme activity. The enzyme has Km for p-nitrophenyl beta-D-galactoside and o-nitrophenyl beta-D-galactoside of 0.56 and 2.0 mM, respectively. The Ki values of galactose and lactose are 2.4 and 70.0 mM, respectively. The energy of activation of PNPG for the enzyme is 10.3 kcal/mol.
D005696:Galactosidases / Q000032:analysis*; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D007526:Isoelectric Point; D007527:Isoenzymes / Q000032:analysis / Q000378:metabolism; D007700:Kinetics; D008670:Metals; D008970:Molecular Weight; D010944:Plants / Q000201:enzymology*; D012639:Seeds / Q000201:enzymology*; D013696:Temperature; D013816:Thermodynamics; D001616:beta-Galactosidase / Q000032:analysis* / Q000037:antagonists & inhibitors / Q000378:metabolism
D007527:Isoenzymes; D008670:Metals; D005696:Galactosidases; D001616:beta-Galactosidase