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Expression of Recombinant Cellulase Cel5A from Trichoderma reesei in Tobacco Plants
Published on: June 13, 2014
Characterization and performance of immobilized amylase and cellulase
Bradley A Saville1, Mikhail Khavkine, Gayathri Seetharam
1Department of Chemical Engineering and Applied Chemistry, University of Toronto, 200 College Street, Toronto, Ontario, Canada M5S 3E5. saville@chem-eng.utoronto.ca
Abstract:
The performance of cellulase and amylase immobilized on siliceous supports was investigated. Enzyme uptake onto the support depended on the enzyme source and immobilization conditions. For amylase, the uptake ranged between 20 and 60%, and for cellulase, 7-10%. Immobilized amylase performance was assessed by batch kinetics in 100-300 g/L of corn flour at 65 degrees C. Depending on the substrate and enzyme loading, between 40 and 60% starch conversion was obtained. Immobilized amylase was more stable than soluble amylase. Enzyme samples were preincubated in a water bath at various temperatures, then tested for activity. At 105 degrees C, soluble amylase lost approximately 55% of its activity, compared with approximately 30% loss for immobilized amylase. The performance of immobilized cellulase was evaluated from batch kinetics in 10 g/L of substrate (shredded wastepaper) at 55 degrees C. Significant hydrolysis of the wastepaper was also observed, indicating that immobilization does not preclude access to and hydrolysis of insoluble cellulose.
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