Optimization of ultrasound-accelerated synthesis of enzymatic caffeic acid phenethyl ester by response surface methodology.
The ultrasound-accelerated enzymatic synthesis of caffeic acid phenethyl ester (CAPE) from caffeic acid and phenethyl alcohol was investigated in this study. A commercial immobilized lipase from Candida antarctica, called Novozym® 435, was used as the catalyst. A 5-level-4-factor central-composite rotatable design (CCRD) and response surface methodology (RSM) were employed to evaluate the effects of reaction time, substrate molar ratio, enzyme amount, and ultrasonic power on percent molar conversion of CAPE. The results indicated that reaction time, substrate molar ratio, and ultrasonic power significantly affected percent molar conversion, whereas enzyme amount did not. A model for synthesis of CAPE was established. Based on ridge max analysis, the optimum condition for CAPE synthesis was predicted to be reaction time 9.6 h, substrate molar ratio 1:71, enzyme amount 2938 PLU, and ultrasonic power 2 W/cm(2) with the molar conversion value of 96.03 ± 5.18%. An experiment was performed under this optimal condition and molar conversion of 93.08 ± 0.42% was obtained.
Chen
Hsiao-Ching
HC
Department of Bioindustry Technology, Dayeh University, Chang-Hua 515, Taiwan.
Chen
Jiann-Hwa
JH
Chang
Cheng
C
Shieh
Chwen-Jen
CJ
D055162:Biocatalysis; D002109:Caffeic Acids / Q000138:chemical synthesis* / Q000737:chemistry; D002175:Candida / Q000201:enzymology; D004800:Enzymes, Immobilized / Q000737:chemistry / Q000378:metabolism*; D005656:Fungal Proteins; D008049:Lipase / Q000737:chemistry / Q000378:metabolism*; D010626:Phenylethyl Alcohol / Q000031:analogs & derivatives* / Q000138:chemical synthesis / Q000737:chemistry; D013499:Surface Properties; D014465:Ultrasonics
D002109:Caffeic Acids; D004800:Enzymes, Immobilized; D005656:Fungal Proteins; C093667:Novozyme 435; D008049:Lipase; C055494:caffeic acid phenethyl ester; D010626:Phenylethyl Alcohol