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Enzyme-catalyzed production of 1-glyceryl benzoate in compressed n-butane
Giovana Ceni1, Patrícia Costa da Silva2, Lindomar Lerin3
1Universidade Federal do Rio de Janeiro, Instituto de Química, Cidade Universitária, 21941-909 Rio de Janeiro, RJ, Brazil; Universidade Regional Integrada do Alto Uruguai e das Missões - URI - Campus de Erechim, Departamento de Engenharia de Alimentos, Av. 7 de Setembro, 1621, 99700-000 Erechim, RS, Brazil.
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 313.15-343.15K and pressures up to 12MPa, 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 5.5wt% of enzyme, methyl benzoate to glycerol molar ratio of 3:1, 50°C and 6h of reaction, affording about 6% of 1-glyceryl benzoate yield.
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