Chaibakhsh_2010_Biotechnol.J_5_848

Reference

Title : Lipase-catalyzed dimethyl adipate synthesis: Response surface modeling and kinetics - Chaibakhsh_2010_Biotechnol.J_5_848
Author(s) : Chaibakhsh N , Rahman MB , Basri M , Salleh AB , Abd-Aziz S
Ref : Biotechnol J , 5 :848 , 2010
Abstract :

Dimethyl adipate (DMA) was synthesized by immobilized Candida antarctica lipase B-catalyzed esterification of adipic acid and methanol. To optimize the reaction conditions of ester production, response surface methodology was applied, and the effects of four factors namely, time, temperature, enzyme concentration, and molar ratio of substrates on product synthesis were determined. A statistical model predicted that the maximum conversion yield would be 97.6%, at the optimal conditions of 58.5 degrees C, 54.0 mg enzyme, 358.0 min, and 12:1 molar ratio of methanol to adipic acid. The R(2) (0.9769) shows a high correlation between predicted and experimental values. The kinetics of the reaction was also investigated in this study. The reaction was found to obey the ping-pong bi-bi mechanism with methanol inhibition. The kinetic parameters were determined and used to simulate the experimental results. A good quality of fit was observed between the simulated and experimental initial rates.

PubMedSearch : Chaibakhsh_2010_Biotechnol.J_5_848
PubMedID: 20632329

Related information

Substrate Adipic-acid

Citations formats

Chaibakhsh N, Rahman MB, Basri M, Salleh AB, Abd-Aziz S (2010)
Lipase-catalyzed dimethyl adipate synthesis: Response surface modeling and kinetics
Biotechnol J 5 :848

Chaibakhsh N, Rahman MB, Basri M, Salleh AB, Abd-Aziz S (2010)
Biotechnol J 5 :848