Enantioselective resolution of (R,S)-1-phenylethanol catalyzed by lipases immobilized in starch films

Journal of the Brazilian Chemical Society

Isabel Hoffmann¹  Vanessa D. Silva¹  Maria Da G. Nascimento¹ 

[1] ,Universidade Federal de Santa Catarina Departamento de Química Florianópolis SC ,Brazil

关键词: starch film;    immobilization;    lipases;    enzymatic resolution;   

DOI  :  10.1590/S0103-50532011000800021

来源: SciELO

【 摘 要 】

Lipases from different sources and two mycelium-bound lipases, in a free or immobilized form, in ginger starch film were screened as biocatalysts in the reaction of (R,S)-1-phenylethanol (1) with vinyl acetate and other acylating agents. The effect of various reaction parameters in the resolution of (1) catalyzed by lipase from Burkholderia cepacia (BCL) immobilized in ginger starch film was evaluated (acyl donor type, alcohol:acyl donor molar ratio, temperature and organic solvent). The catalytic efficiency of BCL immobilized in polymeric blends of ginger starch and polyethylene oxide (PEO), in different compositions, was also studied. Vinyl acetate and iso-propenyl acetate furnished the highest conversion (9%) and enantiomeric excess (> 99%) of the (R)-ester. The alcohol:acyl donor molar ratio and temperature optimum were 1:1 and 28 ºC, respectively. The mixture of n-hexane/glycerol (9:1 v:v) was the most adequate for this reaction (conversion 23%, E > 200). The ginger starch/PEO (7:3 m/m) blend was successfully reused six times consecutively.

【 授权许可】

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