CELLULASE BINDING TO CELLULOSE FIBERS IN HIGH-SHEAR FIELDS

Citation
F. Kaya et al., CELLULASE BINDING TO CELLULOSE FIBERS IN HIGH-SHEAR FIELDS, Journal of biotechnology, 36(1), 1994, pp. 1-10
Citations number
20
Categorie Soggetti
Biothechnology & Applied Migrobiology
Journal title
ISSN journal
01681656
Volume
36
Issue
1
Year of publication
1994
Pages
1 - 10
Database
ISI
SICI code
0168-1656(1994)36:1<1:CBTCFI>2.0.ZU;2-G
Abstract
Cellulase binding onto cellulose fiber was investigated in a turbulent mixing environment created by an axial flow impeller. The binding of the enzyme was found to be associated with various process variables s tudied, e.g., intensity of agitation, reaction time, pulp consistency, pH, temperature, and concentration of enzyme. The similarity between trends in enzyme binding and enzyme activity confirmed that the reduct ion of binding with increasing intensity of agitation over time was du e to denaturation of the enzyme by shear. Physical forces like shear c an disrupt the structure of the enzyme resulting in the loss of bindin g ability and activity. It also appeared that mild mixing did not dena ture the enzyme, but rather the enzyme dispersed better into the pulp slurry, resulting in a higher percentage of enzyme bound to fiber. How ever, increasing shear resulted in a reduction in binding and activity . At a low rpm, the binding increased initially with time, reached a p eak at about 3 to 5 min, and then decreased gradually. With respect to time and shear rate, the reduction in binding and activity was much m ore significant at 10 min of mixing. It is concluded that a high shear and/or a prolonged exposure to a low shear can disrupt the structure of enzyme resulting in the loss of binding ability and activity. At lo w enzyme concentrations, the binding of enzyme onto fiber increases wi th increasing concentration of enzyme. Similarly, the percentage of en zyme bound increased with increasing pulp consistency. Since cellulase needs mild temperatures and acidic environments to maintain its activ ity, high temperature and pH caused a reduction in binding. A pH of 4 and a temperature of 30 degrees C yielded the highest percent binding among the conditions studied.