Properties of enzymes immobilized by the diazotized m-diaminobenzene method.
Some properties of a number of enzymes immobilized by the diazotized m-diaminobenzene (dDAB) method are described. The pH-activity profiles of beta-D-glucosidase, glucoamylase, peroxidase, uricase, and D-glucose oxidase were virtually unchanged on immobilization while those of catalase and dextranase were significantly altered. beta-D-Glucosidase, glucoamylase, and glucose oxidase were found to be more susceptible to denaturation on lyophilization when immobilized than in the native state; however, sorbitol had a marked protective effect in every case examined. Sorbitol was also found to exert a stabilizing effect when lyophilized immobilized preparations were stored. Immobilization marginally improved the stabilities of a number of enzymes to heating at 60 degrees at pH 8.0. The usefulness for continuous reaction of a column of glucoamylase attached to celite was established. The reuse of the solid supports was demonstrated.
D000814:Aniline Compounds; D001391:Azo Compounds; D004800:Enzymes, Immobilized / Q000032:analysis / Q000138:chemical synthesis; D005612:Freeze Drying; D006863:Hydrogen-Ion Concentration; D008722:Methods; D013696:Temperature
D000814:Aniline Compounds; D001391:Azo Compounds; D004800:Enzymes, Immobilized