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National Chung Hsing University Institutional Repository - NCHUIR > 學術研究中心 > 生物科技發展中心 > 依資料類型分類 > 期刊論文 >  Lipase catalyzed acetylation of 3,5,40-trihydroxystilbene: optimization and kinetics study

Please use this identifier to cite or link to this item: http://nchuir.lib.nchu.edu.tw/handle/309270000/145829

標題: Lipase catalyzed acetylation of 3,5,40-trihydroxystilbene: optimization and kinetics study
作者: Kuo, Chia-Hung;Hsiao, Fang-Wen;Dai, Shu-Mei;Chieh-Ming, J.Chang;Lee, Chih-Chen;Liu, Yung-Chuan;Shieh, Chwen-Jen
Contributors: Wei Chun Wang
關鍵字: Lipase acetylation;Hydroxystilbene;Optimization;Kinetics;Response surface methodology
日期: 2012-02
Issue Date: 2013-07-02 10:46:26 (UTC+8)
摘要: 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.
Relation: Bioprocess Biosyst Eng, Volume 35, Page(s) 1137–1145.
Appears in Collections:[依教師分類] 張傑明
[依資料類型分類] 期刊論文

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