Abstract
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.
Published Version
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