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In relation to this article, we declare that there is no conflict of interest.
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Received January 8, 2013
Accepted June 9, 2013
articles This is an Open-Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/bync/3.0) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
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Loofah sponge activated by periodate oxidation as a carrier for covalent immobilization of lipase

1State Key Laboratory of Food Science and Technology, Jiangnan University, Wuxi 214122, P. R. China 2College of Life Science, Anhui Normal University, Wuhu 241000, P. R. China
rmgong.nju@163.com
Korean Journal of Chemical Engineering, August 2013, 30(8), 1620-1625(6), 10.1007/s11814-013-0102-z
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Abstract

Cellulose in loofah sponge was first oxidized by sodium periodate at positions 2 and 3 of anhydroglucose unit to introduce aldehyde groups, which were able to react with amino groups of lipase to form Schiff’s base, and result in loofah sponge immobilized lipase. The result of periodate oxidation was confirmed by determination of aldehyde group content and analysis of Fourier transform infrared spectra. The optimal pH for both free and immobilized lipases was approximately 7.5. The maximum activity of immobilized lipase was observed at 40 ℃, while the free lipase exhibited maximum activity at 37 ℃. The immobilized lipase presented improved thermal stability, storage stability, and reusability.

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