1. Immobilization of Laccase for Oxidative Coupling of Trans-Resveratrol and Its Derivatives.
- Author
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Hong Zhang, Erna Xun, Jiaxin Wang, Ge Chen, Tiexin Cheng, Zhi Wang, Tengfei Ji, and Lei Wang
- Subjects
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OXIDATIVE stress , *RESVERATROL , *DRUG derivatives , *LACCASE , *ENZYME activation , *IMMOBILIZED enzymes - Abstract
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. [ABSTRACT FROM AUTHOR]
- Published
- 2012
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