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

^*Korresponderande författare för detta arbete

Forskningsoutput: Tidskriftsbidrag › Artikel › Vetenskaplig › Peer review

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Sammanfattning

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.

Originalspråk	Engelska
Sidor (från-till)	673-683
Antal sidor	11
Tidskrift	Kinetics and Catalysis
Volym	53
DOI	https://doi.org/10.1134/S0023158412060092
Status	Publicerad - nov. 2012
MoE-publikationstyp	A1 Tidskriftsartikel-refererad

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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.",

author = "S. Sahin and P. M{\"a}ki-Arvela and M. Kangas and K. Er{\"a}nen and J. W{\"a}rn{\aa} and T. Salmi and Murzin, {D. Yu}",

year = "2012",

month = nov,

doi = "10.1134/S0023158412060092",

language = "English",

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pages = "673--683",

journal = "Kinetics and Catalysis",

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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

M3 - Article

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SN - 0023-1584

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

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