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

*Korresponderande författare för detta arbete

Forskningsoutput: TidskriftsbidragArtikelVetenskapligPeer review

5 Citeringar (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.

Sidor (från-till)673-683
Antal sidor11
TidskriftKinetics and Catalysis
StatusPublicerad - nov. 2012
MoE-publikationstypA1 Tidskriftsartikel-refererad


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