Thermomyces lanuginosus lipase-catalyzed synthesis of natural flavor esters in a continuous flow microreactor.
Enzymatic catalysis is considered to be among the most environmental friendly processes for the synthesis of fine chemicals. In this study, lipase from Thermomyces lanuginosus (Lecitase Ultra™) was used to catalyze the synthesis of flavor esters, i.e., methyl butanoate and methyl benzoate by esterification of the acids with methanol in a microfluidic system. Maximum reaction rates of 195 and 115 mM min-1corresponding to catalytic efficiencies (kcat/KM) of 0.30 and 0.24 min-1mM-1as well as yield conversion of 54 and 41 % were observed in methyl butanoate and methyl benzoate synthesis, respectively. Catalytic turnover (kcat) was higher for methyl butanoate synthesis. Rate of synthesis and yield decreased with increasing flow rates. For both esters, increase in microfluidic flow rate resulted in increased advective transport over molecular diffusion and reaction rate, thus lower conversion. In microfluidic synthesis using T. lanuginosus lipase, the following reaction conditions were 40 °C, flow rate 0.1 mL min-1, and 123 U g-1enzyme loading found to be the optimum operating limits. The work demonstrated the application of enzyme(s) in a microreactor system for the synthesis of industrially important esters.
Department of Biotechnology and Microbiology, Faculty of Science, Federal University, Dutse, 7156, Jigawa State, Nigeria. dr.gumel@fud.edu.ng.|Faculty of Science, Institute of Biological Sciences, University of Malaya, 50603, Kuala Lumpur, Malaysia. dr.gumel@fud.edu.ng.
Ahmad Mohammed
AM
Gumel
Faculty of Science, Institute of Biological Sciences, University of Malaya, 50603, Kuala Lumpur, Malaysia.
M S M
MSM
Annuar
Biocatalysis; Esterification; Flavor esters; Lecitase Ultra™; Lipases; Microreactor