Co-immobilization Mechanism of Cellulase and Xylanase on a Reversibly Soluble Polymer |
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Authors: | Zidong Xu Yelian Miao Jie Yu Chen Xuejian Jiang Lijun Lin Pingkai Ouyang |
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Institution: | (1) State Key Laboratory of Materials-Oriented Chemical Engineering, College of Food Science and Light Industrial Technology, Nanjing University of Technology, Jiangsu, Nanjing, 210009, China;(2) Faculty of Bioresource Science, Akita Prefectural University, Akita 010-0195, Japan; |
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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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