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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.

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A study on c-Al 2 O 3 supported CuCl 2 /KCl/LaCl 3 for ethane oxychlorination was carried out by means of XRD, XPS,TGA/ DTA, BET TEM and ICP. The experimental results indicate that the catalytic properties of the 5 wt,%Cu-6 wt.%K-5 wt.%La/ c-A1 2 O 3 are optimal. This catalyst was studied in more detail and it was found that deactivation of the catalyst was due to carbon deposition and loss of active species of Cu +2 .