Characterization of Cellulase Immobilized on Dextran and Diethylaminoethyl-dextran
M.r. Momongan | R.m. Castillo | E.j. Del Rosario
Abstract:
Cellulase was covalently bound to water-soluble dextran, by means of 2-amino-4,6-dichloro-s-triazine, and immobilized on diethylaminoethyl (DEAE)dextran via ionic linkage at pH 4.0. The free enzyme had a maximal specific activity, using carboxymethyl-cellulose as substrat"e, at pH 5.0 while the dextranbound and DEAE-dextran-bound enzymes had maximal activites at pH 7.5 and 4.0, respectively. The frei: enzyme was most active at so0c. Oextran-bound and DEAE-dextran-bound cellulase were most active at 55 and 60°c, respectively.
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