Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10233135 | Enzyme and Microbial Technology | 2010 | 7 Pages |
Abstract
The aim of this work is to report the enzymatic transesterification production of 1-glyceryl benzoate in compressed n-butane, using a commercial immobilized lipase, Novozym 435. For this purpose, reaction experiments were performed on the basis of phase equilibrium data of the system methyl benzoate/n-butane, measured using the static synthetic method with a variable-volume view cell in the temperature range of 313.15-343.15 K and pressures up to 12 MPa, in the entire compositional range of n-butane. Results indicate the existence of a relatively complex phase behavior for all temperatures investigated with the occurrence of vapor-liquid and liquid-liquid phase transitions. Reaction results showed that the strategy adopted for the experimental design proved to be useful in optimizing the reaction conversion in pressurized n-butane and Novozym 435. The optimum conditions were found to be 5.5 wt% of enzyme, methyl benzoate to glycerol molar ratio of 3:1, 50 °C and 6 h of reaction, affording about 6% of 1-glyceryl benzoate yield.
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Physical Sciences and Engineering
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Bioengineering
Authors
Giovana Ceni, PatrÃcia Costa da Silva, Lindomar Lerin, Rafael Mengotti Charin, J. Vladimir Oliveira, Geciane Toniazzo, Helen Treichel, Enrique Guillermo Oestreicher, Débora de Oliveira,