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

Autor:	D. Yu. Murzin, Tapio Salmi, J. Wärnnå, Serap Sahin, Kari Eränen, Päivi Mäki-Arvela, Matias Kangas
Rok vydání:	2012
Předmět:	Chromatography Ethanol biology Ethyl acetate General Chemistry Residence time distribution Toluene Catalysis Computer Science Applications Kinetic resolution Acetic acid chemistry.chemical_compound chemistry Modeling and Simulation biology.protein Lipase Nuclear chemistry
Zdroj:	Kinetics and Catalysis. 53:673-683
ISSN:	1608-3210 0023-1584
DOI:	10.1134/s0023158412060092
Popis:	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.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::099fead3e8d0566e0b9082965b023a6a https://doi.org/10.1134/s0023158412060092 Zobrazit plný text záznamu Plný text ve formátu PDF