Co-immobilization Mechanism of Cellulase and Xylanase on a Reversibly Soluble Polymer
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Cellulase and xylanase from Trichoderma reesei were immobilized simultaneously on Eudragit L-100, a reversibly soluble polymer. The effects of polymer concentration and polymer precipitation pH on enzyme activity recovery were investigated at an enzyme complex concentration of 1%. The immobilization mechanism of cellulase and xylanase on the polymer was discussed. An activity recovery of 75% and 59% was obtained for the cellulase and the xylanase, respectively, under the condition of a polymer concentration at 2% and a polymer precipitation pH at 4.0. Most zymoproteins might be connected to the polymer by electrostatic attraction in a medium of pH 4.8. In addition, the covalent coupling between the zymoproteins and the polymer was demonstrated by the infrared spectrograms. It was suggested that dehydration–condensation reaction occurred between the zymoproteins and the polymer during the immobilization.
KeywordsImmobilization Cellulase Xylanase Covalent coupling Ionic adsorption
This research project was financially supported by a grant of the National Natural Science Foundation of China and the People’s Government of Guangdong Province (U0733001) and a grant of National Basic Research Program of China (973 Program, 2009CB724700). The authors would like to thank Novozymes Investment for providing the commercial enzyme complex.
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