Regioselective acylation of pyridoxine catalyzed by immobilized lipase in ionic liquid

Frontiers of Chemical Engineering in China - Tập 2 - Trang 301-307 - 2008
Shu Bai1, Mengyuan Ren1, Lele Wang1, Yan Sun1
1Department of Biochemical Engineering, School of Chemical Engineering and Technology, Tianjin University, Tianjin, China

Tóm tắt

The regioselective acylation of pyridoxine catalyzed by immobilized lipase (Candida Antarctica) in 1-butyl-3-methylimidazolium hexafluorophosphate ([BMIM]PF6) has been investigated, and compared with that in acetonitrile (ACN). The acetylation of pyridoxine using acetic anhydride in [BMIM]PF6 gave comparable conversion of pyridoxine to 5-monoacetyl pyridoxine with considerably higher regioselectivity (93%–95%) than that in ACN (70%–73%). Among the tested parameters, water activity (a w) and temperature have profound effects on the reaction performances in either [BMIM]PF6 or ACN. For the reaction in [BMIM] PF6, higher temperature (50°C–55°C) and lower a w (<0.01) are preferable conditions to obtain better conversion and regioselectivity. Mass transfer limitation and intrinsic kinetic from the ionic nature of ionic liquids (ILs) may account for a different rate-temperature profile and a lower velocity at lower temperature in [BMIM]PF6-mediated reaction. Moreover, consecutive batch reactions for enzyme reuse also show that lipase exhibited a much higher thermal stability and better reusability in [BMIM]PF6 than in ACN, which represents another advantage of ILs as an alternative to traditional solvents beyond green technology.

Tài liệu tham khảo

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