[Enzymatic properties of immobilized beta-galactosidase from Curvularia inaequalis].
beta-Galactosidase (EC 3.2.1.23) from fungus Curvularia inaequalis was modified by active brilliant orange KH and adsorbed on DEAE-Sephadex A-50. The lactose hydrolysis was studied in a continous flow on the column packed with the immobilized enzyme. The pH and temperatures optima for the substrate hydrolysis by the immobilized enzyme were shown to remain unchanged. A certain destabilizing effect of the matrix on the enzyme resistance to hear denaturation was observed. The activation parameters of denaturation of the native enzyme as well as those of the dye-modified and immobilized preparations were determined.
D055598:Chemical Phenomena; D002621:Chemistry; D004396:Coloring Agents; D004789:Enzyme Activation; D004800:Enzymes, Immobilized; D005696:Galactosidases / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D003904:Mitosporic Fungi / Q000201:enzymology*; D011489:Protein Denaturation; D013696:Temperature
D004396:Coloring Agents; D004800:Enzymes, Immobilized; D005696:Galactosidases
Fermentativnye svoĭstva immobilizovannoĭ beta-galaktozidazy iz Curvularia inaequalis