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Updated: Jun 11, 2026

Investigating Receptor-ligand Systems of the Cellulosome with AFM-based Single-molecule Force Spectroscopy
Published on: December 20, 2013
Co-immobilization mechanism of cellulase and xylanase on a reversibly soluble polymer
Zidong Xu1, Yelian Miao, Jie Yu Chen
1State Key Laboratory of Materials-Oriented Chemical Engineering, College of Food Science and Light Industrial Technology, Nanjing University of Technology, Jiangsu, Nanjing, China.
Abstract:
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.
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