Abstract
Endo-β-1,4-xylanase derived from Trichoderma reesei was covalently immobilized on poly (ethylene glycol) methyl ether 5000 (mPEG5000), and the resulting immobilized enzyme had a residual activity of 72.4 % with 82.9 % of PEGylated amino groups. Compared with the free enzyme, the immobilized xylanase was stable at pH values in the range of 4.0–6.0 and temperatures in the range of 50–65 °C. A self-extractive bioconversion system composed of immobilized xylanase, mPEG5000, and sodium citrate was used to produce xylo-oligosaccharides and provided a better distribution of the xylo-oligosaccharides than the free enzyme. Furthermore, the immobilized xylanase could be effectively recovered in situ following the hydrolysis reaction.
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Acknowledgments
The authors would like to acknowledge the financial support received from the Key Technology R&D Program of Jiangsu Province of China (grant no. BE2010732), the Natural Science Foundation of Jiangsu Province (grant no. BK20131426), the National Natural Science Foundation of China (grant no. 31000278), the Research Fund for the Doctoral Program of Higher Education of China (grant no. 20103204120009), the Excellent Youth Foundation of Jiangsu Province of China (grant no. BK2012038), and the Priority Academic Program Development of the Jiangsu Higher Education Institutions.
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Li, X., Shan, Z., Song, X. et al. Immobilization of Xylanase on Poly (Ethylene Glycol) Methyl Ether 5000 and its Self-Extractive Bioconversion for the Production of Xylo-Oligosaccharides. Appl Biochem Biotechnol 172, 2022–2029 (2014). https://doi.org/10.1007/s12010-013-0666-4
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DOI: https://doi.org/10.1007/s12010-013-0666-4