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

• Main Authors: Tiexin Cheng, Zhi Wang, Tengfei Ji, Lei Wang, Ge Chen, Hong Zhang, Jiaxin Wang, Erna Xun
• Format: Article
• Language: English
• Published: MDPI AG 2012-05-01
• Series: International Journal of Molecular Sciences
• Subjects: laccase; SBA-15; immobilization; oxidative coupling; resveratrol
• Online Access: http://www.mdpi.com/1422-0067/13/5/5998

<em>Trametes villosa</em> Laccase<em> </em>(TVL)<em> </em>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.