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- W2079676557 abstract "Enzymatic hydrolysis of a mixture of (chloromethyldimethylsilyl)-2-propenyl acetate isomers was investigated by using immobilized Candida antarctica lipase as biocatalyst. TLC analysis and 1H NMR spectroscopy were used to monitor the extent of the reaction. At 60 °C, the enzyme exhibited a high selectivity towards 3-(chloromethyldimethylsilyl)-2-propenyl acetate which was almost quantitatively hydrolyzed, whereas, only 11% of 2-(chloromethyldimethylsilyl)-2-propenyl acetate reacted with the lipase. Consequently, the unreacted acetate was readily purified from the reaction medium by flash column chromatography and deacetoxylated in acidic methanol to give the corresponding hydroxy compound in a 71% global yield. On the other hand, without lipase, chemical treatment of the acetate mixture resulted in much lower yields in hydroxy compounds followed by a tedious purification process." @default.
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- W2079676557 date "2001-11-01" @default.
- W2079676557 modified "2023-10-18" @default.
- W2079676557 title "Enzymatic hydrolysis of (chloromethyldimethylsilyl)-2-propenyl acetate isomers: atypic specificity of Candida antarctica lipase" @default.
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- W2079676557 doi "https://doi.org/10.1016/s0168-1656(01)00364-9" @default.
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