Lipase catalyzed acetylation of 3,5,40-trihydroxystilbene: optimization and kinetics study

• Published in: Bioprocess and Biosystems Engineering
• Main Authors: Kuo, Chia-Hung, Hsiao, Fang-Wen, Dai, Shu-Mei, Chieh-Ming, J.Chang, Lee, Chih-Chen, Liu, Yung-Chuan, Shieh, Chwen-Jen
• Other Authors: Wei Chun Wang
• Format: Article in Journal/Newspaper
• Language: English
• Published: 2012
• Subjects: Lipase acetylation; Hydroxystilbene; Optimization; Kinetics; Response surface methodology; Antarc*; Antarctica
• Online Access: http://hdl.handle.net/11455/63353; https://doi.org/10.1007/s00449-012-0698-0

The use of immobilized lipase from Candida antarctica (Novozym 435) to catalyze acetylation of trans-3,5,40-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-40-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-40-O-acetyl-3,5- dihydroxystilbene. The reaction kinetics was found to follow the Ping-Pong mechanism; substrate inhibition was not found at high vinyl acetate concentration.