Synthesis of neryl acetate by free lipase-catalyzed transesterification in organic solvents and its kinetics

Abstract

In this paper, the optimum conditions and kinetics of lipase-catalyzed transesterification reaction of nerol and vinyl acetate for the synthesis of neryl acetate were investigated in a solvent-free system. The optimum conditions were determined as follows: the reaction temperature was 40 °C, the amount of enzyme was 12 mg/mL, and there was no need to add water. Increasing the stirring speed to 200 r/min can eliminate the external diffusion limitations. There was no substrate inhibition when the substrate concentration was lower than 500 mmol/L. However, the experimental results indicated that the product inhibition effect should be considered. The results of the reaction kinetic analysis indicated that the reaction followed the ping-pong double-double reaction mechanism with product inhibition. Finally, the model parameters were calculated by MATLAB software and the results showed that the experimental values could be in good agreement with the simulated values, and the relative error was 6.98%.

Enhanced Enzymatic Performance of Immobilized Pseudomonas fluorescens Lipase on ZIF-8@ZIF-67 and Its Application to the Synthesis of Neryl Acetate with Transesterification Reaction

“…After the above optimization, the yield of neryl acetate could reach over 99% after 3 h of reaction. This was a significant improvement on our previous study [27], and although the final yield of neryl acetate was almost the same, the reaction time was greatly reduced. In contrast to other literature, Zong et al [47] successfully produced neryl acetate by biosynthesis using recombinant Escherichia coli.…”

“…The results indicated that the optimal reaction temperature for the immobilized enzyme to catalyze the reaction was 50 °C. Compared to the optimal reaction temperature of 40 °C for the free enzyme [ 27 ], it increased by 10 °C. This also indicated that the thermal stability of the immobilized enzyme was greatly improved compared to that of the free enzyme.…”

“…With increasing temperature, the initial reaction speed increased and then decreased, while the yield of neryl acetate continuously increased and finally stabilized. The initial reaction rate and yield were highest at 50 • C. When the temperature reached 60 • C, the initial rate decreased, and the final conversion rate was similar to that at 50 • C. The results indicated that the optimal reaction temperature for the immobilized enzyme to catalyze the reaction was 50 • C. Compared to the optimal reaction temperature of 40 • C for the free enzyme [27], it increased by 10 • C. This also indicated that the thermal stability of the immobilized enzyme was greatly improved compared to that of the free enzyme. This is because the rigidity of the enzyme increases after it is immobilized on the carrier.…”

“…In addition, certain concentrations of neryl acetate have insecticidal activity and are widely used to control corn weevil [ 25 ]. In the study of neryl acetate preparation, its efficient synthesis using the lipase-catalyzed transesterification reaction is an important direction of current research [ 26 , 27 ].…”

Studies on the highly efficient catalyzation of sesamin to asarinin by phosphotungstic acid

“…The reaction kinetic is very important both for understanding the fundamental reaction mechanism and for practical production (Sun et al, 2022;Xiong et al, 2022). Isomerization of sesamin to asarinin is a reversible reaction as schemed in Figure 1.…”