Solvent Free Lipase Catalysed Synthesis of Ethyl Laurate: Optimization and Kinetic Studies.
The current research work represents solvent free enzymatic synthesis of fatty acid ethyl ester; ethyl laurate. Immobilized lipase Fermase CALB™10,000 was used for the synthesis of ethyl laurate from ethanol and lauric acid. The influence of process parameters such as catalyst loading, speed of agitation, mole ratio, molecular sieves and temperature were studied. Fermase CALB™10,000 offered a conversion of 92.46 % at 60 °C in 4 h at optimized condition. The experimental data was best fitted by the Random Bi-Bi model with inhibition of both the substrates i.e. lauric acid and ethanol. The following kinetic parameters were retrieved from the model: Vmax = 1.243 × 103 mmol/min/g enzyme; KA = 0.1283 mmol; KB = 8.51 mmol; KiA = 5.098 mmol; and SSE = 0.0142. The activation energy for the enzymatic esterification was also determined and calculated to be 28.49 kJ/mol. A maximum conversion of 71 % was obtained after 5 successive reuse of Fermase CALB™10,000 lipase.
['Gawas|Sarita D|SD|', 'Jadhav|Sachin V|SV|', 'Rathod|Virendra K|VK|']
D061249:Batch Cell Culture Techniques D055162:Biocatalysis D019149:Bioreactors D002175:Candida D000431:Ethanol D057446:Hydrodynamics D007700:Kinetics D007848:Laurates D007850:Lauric Acids D008049:Lipase D059027:Recycling D012997:Solvents D013696:Temperature D013997:Time Factors
Lipase Random Bi-Bi model Biocatalysis Flavour Solvent free system