화학공학소재연구정보센터
Catalysis Today, Vol.375, 120-131, 2021
Green synthesis of amyl levulinate using lipase in the solvent free system: Optimization, mechanism and thermodynamics studies
The current research work focuses on the conventional bio-catalysed synthesis of amyl levulinate with immobilized Candida antarctica lipase B in the absence of a toxic solvent. The green catalyst and solvent free system offered considerable benefits like mild and gentle condition requirement, lesser-energy demand, easy downstreaming and reusability of the biocatalyst. The process parameters were examined, and the maximum conversion (73.2 %) was obtained under the optimum condition of 50celcius temperature, 1:3 M ratio of levulinic acid to amyl alcohol using 0.8 % (w/v) biocatalyst at 250 rpm speed. The immobilized lipase was characterized by SEM, BET, XRD, FTIR and amyl levulinate was characterized by FTIR and GC-MS analysis. The enzyme lipase was effectively reused till 5 cycles for the formation of ester. The thermodynamic parameters (delta H, delta G, and delta S) and energy of activation (Ea) were determined for the assessment of energy requirement. The activation energy was determined to be 48.42 kJ/mol. The research protocol strikes the development of biocatalytic synthetic route of amyl levulinate without using any toxic solvent, which may contribute to green chemistry approach.