Optimization of lipase-catalyzed synthesis of sorbitan acrylate using response surface methodology.
In this study, we have synthesized sorbitan acrylate through response surface methodology, using sorbitan and vinyl acrylate that catalyze immobilized lipase. In order to optimize the enzymatic synthesis of the sorbitan acrylate, we applied response surface techniques to determine the effects of five-level-four-factors and their reciprocal interactions with the biosynthesis of sorbitan acrylate. Our statistical model predicted that the highest conversion yield of sorbitan acrylate would be approx 100%, under the following optimized reaction conditions: a reaction temperature of 40.1 degrees C, a reaction time of 237.4 min, an enzyme concentration of 8%, and a 4.49:1 acyl donor/acceptor molar ratio. Using these optimal conditions in three independent replicates, the conversion yield reached 97.6+/-1.3%.
Jeong
Gwi-Taek
GT
School of Biological Sciences and Technology, Chonnam National University, 500-757, Gwangju, Korea.
Park
Don-Hee
DH
D000179:Acrylates / Q000138:chemical synthesis*; D002384:Catalysis; D020650:Combinatorial Chemistry Techniques / Q000379:methods*; D004800:Enzymes, Immobilized; D004951:Esterification; D005656:Fungal Proteins; D008049:Lipase / Q000737:chemistry*; D011136:Polysorbates / Q000138:chemical synthesis*; D011786:Quality Control
D000179:Acrylates; D004800:Enzymes, Immobilized; D005656:Fungal Proteins; D011136:Polysorbates; C093667:Novozyme 435; D008049:Lipase