1. Highly Efficient Enzymatic Acylation of Dihydromyricetin by the Immobilized Lipase with Deep Eutectic Solvents as Cosolvent.
- Author
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Cao SL, Deng X, Xu P, Huang ZX, Zhou J, Li XH, Zong MH, and Lou WY
- Subjects
- Acylation, Aspergillus niger chemistry, Enzymes, Immobilized chemistry, Enzymes, Immobilized metabolism, Flavonols metabolism, Fungal Proteins metabolism, Lipase metabolism, Oxidation-Reduction, Aspergillus niger enzymology, Flavonols chemistry, Fungal Proteins chemistry, Lipase chemistry
- Abstract
A novel deep eutectic solvent (DES)-DMSO cosolvent system has been, for the first time, successfully used as the reaction medium for the enzymatic acylation of dihydromyricetin (DMY) catalyzed by the immobilized lipase from Aspergillus niger (ANL). The cosolvent mixture, ChCl:Glycerol-DMSO (1:3, v/v) proved to be the optimal medium. With the newly developed cosolvent, the initial reaction rate of enzymatic acylation of DMY achieved 11.1 mM/h and the conversion of DMY was 91.6%. ANL@PD-MNPs is stable and recyclable in this cosolvent, offering 90% conversion rate after repeated use of 5 times. The lipid-solubility of DMY-16-acetate was 10 times higher than that of its raw materials DMY. The results showed that the DMY-16-acetate product exhibits good antioxidative activity. The present research illustrated that the use of DES-DMSO cosolvent may become a feasible alternative for the synthesis of DMY ester.
- Published
- 2017
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