Enzyme-catalyzed production of 1-glyceryl benzoate in compressed n-butane

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.