Asymmetric Hydrolysis of (dl)-1-Acyloxy-2-halo-1-phenylethanes with Lipases
1986 年 50 巻 9 号 p. 2369-2373
詳細
1986 年 50 巻 9 号 p. 2369-2373
Asymmetric hydrolysis of (dl)-1-acyloxy-2-halo-1-phenylefhanes by lipoprotein lipase Amano P from Pseudomonas fluorescens and the lipase from Chromobacterium viscosum afforded the optically active (R) residual substrates and (S)-2-halo-1-hydroxy-1-phenylethanes in 100% enantiomeric excess (e.e.). The length of acyl residues from acetyl to octanoyl in the substrates did not influence the enantioselectivity.
Both enantiomers of optically active styrene oxides were synthesized from the enzymatic products.
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