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Int. J. Mol. Sci. 2012, 13(5), 5998-6008; doi:10.3390/ijms13055998

Immobilization of Laccase for Oxidative Coupling of Trans-Resveratrol and Its Derivatives

2,* , 3,*  and 2,*
1 College of Chemistry, Jilin University, Changchun 130023, China 2 Key Laboratory of Molecular Enzymology and Engineering of Ministry of Education, College of Life Sciences, Jilin University, Changchun 130023, China 3 State Key Laboratory of Bioactive Substances and Functions of Natural Medicines, Institute of Materia Medica, Chinese Academy of Medical Sciences and Peking Union Medical College, Beijing 100050, China
* Authors to whom correspondence should be addressed.
Received: 5 April 2012 / Revised: 4 May 2012 / Accepted: 9 May 2012 / Published: 18 May 2012
(This article belongs to the Special Issue Enzyme Optimization and Immobilization)
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Trametes villosa Laccase (TVL) was immobilized through physical adsorption on SBA-15 mesoporous silica and the immobilized TVL was used in the oxidative coupling of trans-resveratrol. Higher loading and activity of the immobilized enzyme on SBA-15 were obtained when compared with the free enzyme. The effects of reaction conditions, such as buffer type, pH, temperature and substrate concentration were investigated, and the optimum conditions were screened and resulted in enzyme activity of up to 10.3 μmol/g·h. Furthermore, the oxidative couplings of the derivatives of trans-resveratrol were also catalyzed by immobilized TVL. The immobilized TVL was recyclable and could maintain 78% of its initial activity after reusing it four times.
Keywords: laccase; SBA-15; immobilization; oxidative coupling; resveratrol laccase; SBA-15; immobilization; oxidative coupling; resveratrol
This is an open access article distributed under the Creative Commons Attribution License (CC BY 3.0).

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Zhang, H.; Xun, E.; Wang, J.; Chen, G.; Cheng, T.; Wang, Z.; Ji, T.; Wang, L. Immobilization of Laccase for Oxidative Coupling of Trans-Resveratrol and Its Derivatives. Int. J. Mol. Sci. 2012, 13, 5998-6008.

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