Lipase-catalyzed acylation in a continuous down-flow fixed-bed reactor

S. Sahin*, P. Mäki-Arvela, M. Kangas, K. Eränen, J. Wärnå, T. Salmi, D. Yu Murzin

*Corresponding author for this work

Research output: Contribution to journalArticleScientificpeer-review

6 Citations (Scopus)


The kinetic resolution of racemic 1-phenylethanol with ethyl acetate was investigated in a down-flow fixed-bed reactor operated in a continuous mode mainly at the molar ratio of 1 : 3 in 400 mL toluene at 70°C. The catalytic activity of the immobilized lipase was studied by: (i) changing the flow rates, (ii) utilizing different substrate concentrations, (iii) applying step changes using ethyl acetate, ethyl benzene, acetic acid, acetophenone etc., (iv) investigating the inhibitory effect of either the desired or the stoichiometric products (R)-1-phenylethyl acetate and ethanol, respectively), (v) elucidating the effect of water on the activity and stability of the immobilized lipase. The residence time distribution and the reactor hydrodynamics were also discussed along with kinetic modelling. The results were linked to the one-pot reactions.

Original languageEnglish
Pages (from-to)673-683
Number of pages11
JournalKinetics and Catalysis
Publication statusPublished - Nov 2012
MoE publication typeA1 Journal article-refereed


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