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Immobilization of β‐galactosidase and other enzymes onto p ‐amino‐carbanilated cellulose derivatives
Author(s) -
Beddows C. G.,
Mirauer R. A.,
Guthrie J. T.
Publication year - 1980
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/bit.260220206
Subject(s) - glutaraldehyde , papain , cellulose , chemistry , diazo , trypsin , enzyme , immobilized enzyme , biochemistry , pepsin , escherichia coli , chromatography , organic chemistry , gene
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.