Lyophilized mycelia of Aspergillus oryzae CBS 102.07, Aspergillus oryzae MIM, Rhizopus oryzae CBS 112.07, Rhizopus oryzae CBS 391.34, Rhizopus oryzae CBS 260.28 and Rhizopus oryzae CBS 328.47 were tested in this study to select the best biocatalysts for ethanol acylation with phenylacetic acid. The mycelium-bound carboxylesterase activity of A. oryzae MIM, which exhibited the best performances, was initially investigated at 50 degrees C, either in 0.1 M phosphate buffer or in n-heptane to catalyse the hydrolysis or the synthesis, respectively, of ethyl phenylacetate. The results in terms of product and substrate concentrations versus time were used to estimate the maximum molar conversions at equilibrium, the equilibrium constants, and the times needed to reach half maximum conversions, thus providing sufficient information about this biotransformation. The values of the apparent equilibrium constants, estimated at 20 degrees C< T< 50 degrees C, were finally used to estimate the thermodynamic parameters of ethanol acylation by this biocatalyst.

Synthesis of ethyl phenylacetate by lyophilized mycelium of Aspergillus oryzae / A. Converti, R. Gandolfi, M. Zilli, F. Molinari, L. Binaghi, P. Perego, M. Del Borghi. - In: APPLIED MICROBIOLOGY AND BIOTECHNOLOGY. - ISSN 0175-7598. - 67:5(2005), pp. 637-640.

Synthesis of ethyl phenylacetate by lyophilized mycelium of Aspergillus oryzae

R. Gandolfi
Secondo
;
F. Molinari;
2005

Abstract

Lyophilized mycelia of Aspergillus oryzae CBS 102.07, Aspergillus oryzae MIM, Rhizopus oryzae CBS 112.07, Rhizopus oryzae CBS 391.34, Rhizopus oryzae CBS 260.28 and Rhizopus oryzae CBS 328.47 were tested in this study to select the best biocatalysts for ethanol acylation with phenylacetic acid. The mycelium-bound carboxylesterase activity of A. oryzae MIM, which exhibited the best performances, was initially investigated at 50 degrees C, either in 0.1 M phosphate buffer or in n-heptane to catalyse the hydrolysis or the synthesis, respectively, of ethyl phenylacetate. The results in terms of product and substrate concentrations versus time were used to estimate the maximum molar conversions at equilibrium, the equilibrium constants, and the times needed to reach half maximum conversions, thus providing sufficient information about this biotransformation. The values of the apparent equilibrium constants, estimated at 20 degrees C< T< 50 degrees C, were finally used to estimate the thermodynamic parameters of ethanol acylation by this biocatalyst.
Settore CHIM/11 - Chimica e Biotecnologia delle Fermentazioni
2005
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2434/11394
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