Enzymatic Amidation and Alkoxycarbonylation of Amines using Native and Immobilised Lipases with Different Origins: a Comparative Study

Enzymatic alkoxycarbonylation with vinyl carbonates and racemic amines can provide chiral carbamates. In the present paper, we have investigated the catalytic potential of some commercial lipases, with different origins. We have used the alkoxycarbonylation of (R,S)-1-phenylethylamine, analysing the influence on the yield and enantioselectivity of some characteristics of the biocatalyts, such as the origin of the lipase and whether the lipase is immobilised or not. We have also investigated the influence on the yield of the chain length of the vinyl carbonate used as the acyl donor. Finally, we have probed this reaction, under the same conditions, with the chiral amines substituted in the aromatic ring, using p-chloro and p-methoxy-1-phenylethylamine and butyl vinyl carbonate.