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

International Journal of Molecular Sciences

Hong Zhang²  Erna Xun¹  Jiaxin Wang¹  Ge Chen¹  Tiexin Cheng²  Zhi Wang¹  Tengfei Ji³ 

[1] Key Laboratory of Molecular Enzymology and Engineering of Ministry of Education, College of Life Sciences, Jilin University, Changchun 130023, China; E-Mails:;College of Chemistry, Jilin University, Changchun 130023, China; E-Mails:;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

关键词: laccase;    SBA-15;    immobilization;    oxidative coupling;    resveratrol;   

DOI  :  10.3390/ijms13055998

来源: mdpi

【 摘 要 】

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.

【 授权许可】

CC BY   
© 2012 by the authors; licensee Molecular Diversity Preservation International, Basel, Switzerland.