抄録
Lipase-catalyzed acetylation of 1-alkanol with vinyl acetate to give alkyl acetate has been studied kinetically using Burkholderia cepacia lipase, six alcohols and different organic solvents. The rate constants kA and kB with respect to vinyl acetate and 1-alkanol determined from the double reciprocal plots, v-1 vs. [vinyl acetate]-1 and v-1 vs. [1-alkanol]-1 respectively, where v is the initial rate of the reaction. The rate ratio kB/kA was larger than unity except some cases: the rate in acetylation of active serine residue in the lipase with vinyl acetate was slower than that of 1-alkanol with the acetyl-enzyme intermediate. The rate constant kA was independent of the solvent hydrophobicity log P (where P is a partition coefficient of a given solvent between octanol and water), however, kB increased with log P. Both rate constants were different depending on the structure (carbon number CN) of 1-alkanol.
