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Immobilization of cellulolytic and hemicellulolytic enzymes on inorganic supports
Author(s) -
Shimizu K.,
Ishihara M.
Publication year - 1987
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.260290214
Subject(s) - cellulase , chemistry , glutaraldehyde , trichoderma viride , carboxymethyl cellulose , xylan , immobilized enzyme , hydrolysis , aspergillus niger , cellulose , enzyme , chromatography , nuclear chemistry , organic chemistry , biochemistry , food science , sodium
Commercial cellulase preparations from Trichoderma viride and Aspergillus niger were immobilized on porous silica glass and ceramics such as alumina and titania with titanium tetrachloride (TiCl 4 ) and on their silanized derivatives with glutaraldehyde (GLUT). The amounts of the immobilized enzymes were in the range 10–50 mg/g carrier (dry) depending on the kind of carrier and immobilization method. Their activities toward carboxymethyl cellulose (CMC), xylan, aryl‐β‐glucoside, and aryl‐β‐xyloside were 3–53% of those of the native enzymes. The optimum pH of the enzymes shifted to the acidic side in most cases, whereas the optimum temperatures were nearly the same as those of native ones. The activity of immobilized enzyme preparations towards CMC did not change significantly during continuous operation over a periods of 60 days. Finally, xylan was hydrolyzed with the immobilized enzymes, and the sugars formed were investigated.