Entrapment of beta-galactosidase in polyvinylalcohol hydrogel.
beta-Galactosidase isolated from Aspergillus oryzae was immobilized in lens-shaped polyvinylalcohol capsules (with activity 25 U g(-1)) giving 32% of its original activity. Immobilization did not change the pH optimum (4.5) of lactose hydrolysis. The relative enzyme activity during product inhibition testing was, in average, 10% higher for immobilized enzyme. No decrease of activity was observed after 35 repeated batch runs and during 530 h of continuous hydrolysis of lactose (10%, w/v) at 45 degrees C. The immobilized enzyme was stable for 14 months without any change of activity during the storage at 4 degrees C and pH 4.5.
Grosová
Zuzana
Z
Institute of Biotechnology and Food Science, Faculty of Chemical and Food Technology, Slovak University of Technology, Radlinského 9, 812 37 Bratislava, Slovak Republic.
Rosenberg
Michal
M
Rebros
Martin
M
Sipocz
Matej
M
Sedlácková
Barbora
B
D002851:Chromatography, High Pressure Liquid; D004795:Enzyme Stability; D004800:Enzymes, Immobilized / Q000737:chemistry / Q000378:metabolism*; D020136:Hydrogel, Polyethylene Glycol Dimethacrylate; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D007785:Lactose / Q000378:metabolism; D011142:Polyvinyl Alcohol / Q000737:chemistry*; D001616:beta-Galactosidase / Q000737:chemistry / Q000378:metabolism*
D004800:Enzymes, Immobilized; D020136:Hydrogel, Polyethylene Glycol Dimethacrylate; D011142:Polyvinyl Alcohol; D001616:beta-Galactosidase; D007785:Lactose