Optimized synthesis of lipase-catalyzed octyl caffeate by Novozym® 435
2010
Chen, Hsiao-Ching | Twu, Yawo-Kuo | Chang, Chieh-ming J. | Liu, Yung-Chuan | Shieh, Chwen-Jen
In this study, optimization of the enzymatic synthesis of octyl caffeate (OC), catalyzed by an immobilized lipase (Novozym® 435) from Candida antarctica was investigated. Novozym® 435 was used to catalyze the caffeic acid and octanol in an isooctane system. Response surface methodology (RSM) and 5-level-4-factor central-composite rotatable design (CCRD) were employed to evaluate the effects of the synthesis parameters, such as reaction temperature (40-80°C), reaction time (24-72h), substrate molar ratio of caffeic acid to octanol (1:20-1:100), and enzyme amounts (100-500PLU) on the percentage conversion of OC by direct esterification. Reaction temperature and time had significant effects on the percent conversion. Based on ridge max analysis, the optimum conditions for synthesis were: reaction time of 55h, reaction temperature of 75°C, substrate molar ratio of 1:78, and enzyme amount of 317PLU. The molar conversions of predicted and actual experimental values were 93.79% and 90.34±1.38%, respectively.
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