A simple room temperature-static bioreactor for effective synthesis of hexyl acetate

Abstract

AbstractFor green synthesis in organic phases, the catalysis of lipases needs to be further improved. Here a strategy is to simulate the activation of lipases at water/oil interface by immobilizing lipase on an available carrier material, which can replace the water at the interface to stabilize enzyme against denaturation from organic phase. The carrier is selected as cotton fiber on which Pseudomonas cepacia lipase is immobilized by physical adsorption in a column glass bottle to form a simple bioreactor together with the bottle. In synthesis of fragrance ester hexyl acetate via transesterification of hexanol with vinyl acetate, the bioreactor exhibits a 3-fold increase in the ability to transform substrate, relative to native lipase in terms of the initial period of reaction at 37°C and 160 rpm. And also the bioreactor is very stable in catalysis for that it has an extra long half life t1/2 = 636 h, calculated from the decrease degree of molar conversions in six times of 6-hour transesterifications. More interestingly, the bioreactor behaves excellent activity at room temperature and in a static state, and can transform nearly 100% hexanol after 48 h. All these indicate that the bioreactor has great potential for industrial application.