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: Iglesias, L.E., Baldessari, A.
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.