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Updated: Apr 20, 2026

Light-driven Enzymatic Decarboxylation
Published on: May 22, 2016
Process optimization and kinetic evaluation for biosynthesis of D-isoascorbyl stearate
Zhenfeng Liu1, Yanmin Shen, Weiwei Li
1School of Chemical Engineering and Energy, Zhengzhou University, Zhengzhou, 450001, China, zhenfeng2083@163.com.
Abstract:
The synthesis of D-isoascorbyl stearate from D-isoascorbic acid and stearic acid with immobilized lipase (Novozym(®)435) as catalyst was studied. Response surface methodology and Box-Behnken design with six variables and three levels were employed to evaluate the effects of processing conditions on the conversion of D-isoascorbic acid. The results confirmed that the response surface method and statistical analysis were proved to be useful in developing optimal conditions for D-isoascorbyl stearate synthesis. The optimum conditions were predicted as follows: reaction temperature 48 °C, reaction time 17.7 h, immobilized lipase amount 50.0 % (w/w, of D-isoascorbic acid), substrate molar ratio 9:1 (stearic acid to D-isoascorbic acid), D-isoascorbic acid concentration 0.14 mol/L (based on solvent), 4A molecular sieve addition 200 g/L (based on solvent), and the optimal conversion was 90.6 %. Through the kinetics model fitting of the esterification, it was considered that the esterification conformed to a Ping-Pong bi-bi kinetic model with D-isoascorbic acid inhibition, and the obtained kinetic constants showed that the inhibition of D-isoascorbic acid and the enzyme affinity to substrate were abate with the increase of the reaction temperature.
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