Immobilization of beta-galactosidase and other enzymes onto p-amino-carbanilated cellulose derivatives.
beta-Galactosidase and other enzymes were immobilized on p-amino-carbanilated derivatives of cellulose and methylol cellulose using the diazo method and through glutaraldehyde. The optimum conditions for coupling cellulose tri-(p-amino-carbanilate) (CTAC) to beta-galactosidase were established. The diazo coupling method with CTAC gave greater activity than with glutaraldehyde when coupled to beta-galactosidase (Escherichia coli). The stability of the CTAC-beta--galactosidase system was examined. The disubstituted p-amino-carbanilate derivative (CDAC) gave a lower activity, whereas the methylol analog (MCTAC) gave slightly greater activity. The CTAC was also used to immobilize glucose oxidase, trypsin, pepsin, and papain.
D000588:Amines; D002224:Carbanilides; D002482:Cellulose / Q000031:analogs & derivatives*; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D004800:Enzymes, Immobilized; D005696:Galactosidases; D005949:Glucose Oxidase; D008747:Methylcellulose / Q000031:analogs & derivatives; D010206:Papain; D010434:Pepsin A; D014357:Trypsin; D001616:beta-Galactosidase
D000588:Amines; D002224:Carbanilides; D004800:Enzymes, Immobilized; D002482:Cellulose; D008747:Methylcellulose; D005949:Glucose Oxidase; D005696:Galactosidases; D001616:beta-Galactosidase; D014357:Trypsin; D010206:Papain; D010434:Pepsin A