Biosynthesis of myristyl serinate by immobilized Candida antarctica lipase in two-phase system

The significance and novelty of this manuscript is that myristyl serinate was firstly synthesized from myristyl alcohol and l-serine using lipase catalyzed esterification in selected solvents. The effects of reaction system, two-phase system composition, temperature, pH, and reaction time on myristyl serinate ester content in the crude reaction mixture were investigated. The results showed that two-phase could significantly increase the enzymatic interesterification conversion and the optimal ratio of two-phase solvent was 80:20 (dichloromethane:phosphate buffer). The optimal conditions for myristyl serinate enzymatic synthesis were substrate molar ratio of 1:1, Novozym 435 load of 5% (w/w), a solvent dosage of 20 ml, 30 °C and reaction time of 36 h. Myristyl serinate content could reach 72.25% in the reaction system. Myristyl serinate was purified through column chromatography and identified by HPLC/IR/LC-MS/NMR.