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

doi:10.1134/S0023158412060092

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 journal › Article › Scientific › peer-review

6 Citations (Scopus)

Abstract

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 language	English
Pages (from-to)	673-683
Number of pages	11
Journal	Kinetics and Catalysis
Volume	53
DOIs	https://doi.org/10.1134/S0023158412060092
Publication status	Published - Nov 2012
MoE publication type	A1 Journal article-refereed

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title = "Lipase-catalyzed acylation in a continuous down-flow fixed-bed reactor",

abstract = "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.",

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T1 - Lipase-catalyzed acylation in a continuous down-flow fixed-bed reactor

AU - Sahin, S.

AU - Mäki-Arvela, P.

AU - Kangas, M.

AU - Eränen, K.

AU - Wärnå, J.

AU - Salmi, T.

AU - Murzin, D. Yu

PY - 2012/11

Y1 - 2012/11

N2 - 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.

AB - 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.

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U2 - 10.1134/S0023158412060092

DO - 10.1134/S0023158412060092

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VL - 53

SP - 673

EP - 683

JO - Kinetics and Catalysis

JF - Kinetics and Catalysis

ER -

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

Abstract

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