期刊
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
卷 13, 期 5, 页码 5998-6008出版社
MDPI AG
DOI: 10.3390/ijms13055998
关键词
laccase; SBA-15; immobilization; oxidative coupling; resveratrol
资金
- National Natural Science Foundation of China [21172093, 31070708, 21072075]
- Natural Science Foundation of Jilin Province of China [201115039, 201115038]
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 mu mol/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.
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