Lipase-catalyzed alcoholysis of 2-thioacetoxyethyl acetate
Lipase-catalyzed alcoholysis of 2-thioacetoxyethyl acetate is described. Results depended on the biocatalyst, the nucleophile and the substrate/nucleophile ratio. When the reaction of the diester was carried out with one equivalent of 1-octanol under Candida antarctica lipase catalysis, it was found...
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Autores principales: | , |
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Formato: | JOUR |
Acceso en línea: | http://hdl.handle.net/20.500.12110/paper_03650375_v86_n3-6_p203_Iglesias |
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Sumario: | Lipase-catalyzed alcoholysis of 2-thioacetoxyethyl acetate is described. Results depended on the biocatalyst, the nucleophile and the substrate/nucleophile ratio. When the reaction of the diester was carried out with one equivalent of 1-octanol under Candida antarctica lipase catalysis, it was found that 2-mercaptoethyl acetate is mainly obtained through S-acetyl removal. |
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