Thermomyces lanuginosus lipase-catalyzed synthesis of natural flavor esters in a continuous flow microreactor

Abstract

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−1 corresponding to catalytic efficiencies (k cat/K M) of 0.30 and 0.24 min−1 mM−1 as well as yield conversion of 54 and 41 % were observed in methyl butanoate and methyl benzoate synthesis, respectively. Catalytic turnover (k cat) 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−1 enzyme 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.

Enzyme immobilization on photopatterned temperature‐response poly (N‐isopropylacrylamide) for microfluidic biocatalysis

“…An increase in the flow rates decreased the residence time of the reactants . When the flow rate ranged from 1 to 5 µL min −1 , the residence time decreased from 24.3 to 5 min.…”

“…Figure (C) shows the effects of the reaction temperature on the isoquercitrin yield in a microchannel reactor. When the reaction temperature was increased from 30 to 45 °C, steady increases in the naringinase catalytic efficiency and isoquercitrin yield were observed, which were regarded as favorable effects of increasing temperature on the heat transfer and mass transfer in a microchannel . At a temperature of 45 °C, the highest yield of 93.63 ± 1.12% was achieved.…”

“…When the reaction temperature was increased from 30 to 45 ∘ C, steady increases in the naringinase catalytic efficiency and isoquercitrin yield were observed, which were regarded as favorable effects of increasing temperature on the heat transfer and mass transfer in a microchannel. 32 At a temperature of 45 ∘ C, the highest yield of 93.63 ± 1.12% was achieved. In addition, PNIPAAm is a thermoreversible water-soluble polymer, and higher temperatures affect both the solubility and porosity properties of the polymers.…”

“…An increase in the flow rates decreased the residence time of the reactants. 32 When the flow rate ranged from 1 to 5 μL min −1 , the A B C Figure 2. The SEM photos of bulk polymers before (A) and after (B) immobilization, the FTIR spectra of naringin enzyme, PNIPAAm and immobilized enzyme (C) in a photopatterned microchannel.…”

Free and Immobilized Lecitase™ Ultra as the Biocatalyst in the Kinetic Resolution of (E)-4-Arylbut-3-en-2-yl Esters

“…Due to its wide enzymatic activity, the application of Lecitase™ Ultra has been further extended to the production of 2 of 18 flavor low-chain esters i.a. methyl benzoate and methyl butanoate [28] and regioselective hydrolysis of peracetylated mono-and disaccharides to produce key intermediates in the preparation of different glycoderivatives such as oligosaccharides, glycolipids, or glycopeptides [29].…”