Abstract
The use of immobilized lipase from Candida antarctica (Novozym® 435) to catalyze acetylation of trans-3,5,4′-trihydroxystilbene was investigated in this study. Response surface methodology and 5-level-4-factor central composite rotatable design were adopted to evaluate the effects of synthesis variables, including reaction time (24–72 h), temperature (25–65 °C), substrate molar ratio (1:15–1:75), and enzyme amount (600–3,000 PLU) on the percentage molar conversion of trans-4′-O-acetyl-3,5-dihydroxystilbene. The results showed that reaction temperature and enzyme amount were the most important parameters on percentage molar conversion. Based on ridge max analysis, the optimum conditions for synthesis were: reaction time 60 h, reaction temperature 64 °C, substrate molar ratio 1:56 and enzyme amount 2,293 PLU. The molar conversion of actual experimental values was 95% under optimal conditions. The synthesis product was analyzed using HPLC, mass and NMR. The results revealed that the major product was trans-4′-O-acetyl-3,5-dihydroxystilbene. The reaction kinetics was found to follow the **-Pong mechanism; substrate inhibition was not found at high vinyl acetate concentration.
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Kuo, CH., Hsiao, FW., Dai, SM. et al. Lipase catalyzed acetylation of 3,5,4′-trihydroxystilbene: optimization and kinetics study. Bioprocess Biosyst Eng 35, 1137–1145 (2012). https://doi.org/10.1007/s00449-012-0698-0
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DOI: https://doi.org/10.1007/s00449-012-0698-0