Immobilization of Xylan-Degrading Enzymes from Scytalidium thermophilum on Eudragit L-100 |
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Authors: | Ruchi Gaur Lata S K Khare |
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Institution: | (1) Chemistry Department, Indian Institute of Technology, Delhi, Hauz-Khas, New Delhi, 110 016, India;(2) Division of Microbiology, Indian Agriculture Research Institute, New Delhi, 110 012, India |
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Abstract: | Summary Xylanase from Scytalidium thermophilum was immobilized on Eudragit L-100, a pH sensitive copolymer of methacrylic acid and methyl methacrylate. The enzyme was non-covalently
immobilized and the system expressed 70% xylanase activity. The immobilized preparation had broader optimum temperature of
activity between 55 and 65 °C as compared to 65 °C in case of free enzyme and broader optimum pH between 6.0 and 7.0 as compared
to 6.5 in case of free enzyme. Immobilization increased the t1/2 of enzyme at 60 °C from 15 to 30 min with a stabilization factor of 2. The Km and Vmax values for the immobilized and free xylanase were 0.5% xylan and 0.89 μmol/ml/min and 0.35% xylan and 1.01 μmol/ml/min respectively. An Arrhenius plot showed an increased value of activation energy for immobilized xylanase (227 kcal/mol)
as compared to free xylanase (210 kcal/mol) confirming the higher temperature stability of the free enzyme. Enzymatic saccharification
of xylan was also improved by xylanase immobilization. |
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Keywords: | Activation energy Arrhenius plot enzymatic saccharification Eudragit L-100 immobilization Scytalidium thermophilum stabilization factor t1/2 xylanase |
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