Immobilization of β‐galactosidase and other enzymes onto p‐amino‐carbanilated cellulose derivatives

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Abstract
β‐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 β‐galactosidase were established. The diazo coupling method with CTAC gave greater activity than with glutaraldehyde when coupled to β‐galactosidase (Escherichia coli). The stability of the CTAC–β‐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.

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