Research Article | OPEN ACCESS
Immobilization of a 22kDa Xylanase on Eudragit L-100 for Xylo-oligosaccharide Production
1Lifen Hou, 2Xiangyang Sun, 2Jixue Sui and 3Changhe Ding
1Zhengzhou Tourism College, Zhengzhou, Henan 450009
2Henan University of Animal Husbandry and Economy, Zhengzhou, Henan 450011
3Henan University of Technology, Zhengzhou, Henan 450052, China
Advance Journal of Food Science and Technology 2015 6:401-407
Received: September ‎22, ‎2014 | Accepted: October ‎24, ‎2014 | Published: February 25, 2015
Abstract
A commercial xylanase was immobilized on Eudragit L-100 with the recovery activity of 87.3-126.2%. After immobilization, the optimum pH was not changed while its optimum temperature moved from 70 to 75°C. However, the immobilized enzyme did not show a higher thermal stability than the free xylanase. A slightly decrease in the Km values of free enzyme was observed upon immobilization. Meanwhile, Vmax values of the immobilized enzyme were 38% higher than those of the free xylanase. The result of Fluorescence spectroscopy used to probe the changes in the enzyme structure upon immobilization showed minute change and which may result in increase of immobilized enzyme activity. The application of immobilized enzyme hydrolyzing cottonseed husk and corncob pretreated by alkaline peroxide solution was the basically same as the free enzyme. The reusability of immobilized enzyme in the third cycles produced 163 and 126% reducing sugar hydrolyzing cottonseed husk and corncob.
Keywords:
Application, eudragit L-100, immobilization, properties, Xylanase,
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Competing interests
The authors have no competing interests.
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This article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made.
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