Optimization of lipase-catalyzed synthesis of octyl hydroxyphenylpropionate by response surface methodology.
The ability of immobilized lipase Candida antarctica (Novozyme 435) to catalyze the direct esterification of hydroxyphenylpropionic acid and octanol in a solvent-free system was investigated in this study. Response surface methodology (RSM) and five-level-four-factor central composite rotatable design (CCRD) were employed to evaluate the effects of synthesis parameters, such as reaction time, temperature, enzyme amount, and pH memory, on percentage molar conversion of phenolic acid esters. Reaction time, temperature, and enzyme amount were the most important variables. On the basis of canonical analysis and ridge max analysis, the optimum synthesis conditions with 95.9% molar conversion were reaction time of 58.2 h, temperature of 52.9 degrees C, enzyme amount of 37.8% (w/w), and pH memory of pH 7.
Twu
Yawo-Kuo
YK
Department of Bioindustry Technology, Dayeh University, Chang-Hua 51505, Taiwan.
Shih
Ing-Lung
IL
Yen
Yun-Horng
YH
Ling
Yi-Fan
YF
Shieh
Chwen-Jen
CJ
D000975:Antioxidants / Q000378:metabolism*; D002175:Candida / Q000201:enzymology; D004951:Esterification; D006863:Hydrogen-Ion Concentration; D008049:Lipase / Q000378:metabolism*; D008954:Models, Biological; D010636:Phenols / Q000378:metabolism*; D011422:Propionates / Q000378:metabolism*; D013696:Temperature; D013997:Time Factors
D000975:Antioxidants; D010636:Phenols; D011422:Propionates; C498246:octyl hydroxyphenylpropionate; D008049:Lipase