酶催化乳酸铵和乙醇合成乳酸乙酯的研究-生物化工专业毕业论文.docxVIP

酶催化乳酸铵和乙醇合成乳酸乙酯的研究 酶催化乳酸铵和乙醇合成乳酸乙酯的研究 LIPASE-CATALYZED SYNTHESIS OF ETHYL LACTATE FROM AMMONIUM LACTATE AND ETHANOL ABSTRACT A noval process for the ethyl lactate synthesis using ammonium lactate as raw material was evaluated. Firstly, the optimal conditions for the esterification were found to be: molar ratio 24: 1 (ethanol /ammonium lactate), reaction time 24 h, ammonium lactate concentration 0.2 mol/L, temperature 60oC, enzyme concentration 40 (g/mol, ammonium lactate), agitation speed 150 r/min and the water activity 0.12, respectively. Under these conditions, 33.88% of ammonium lactate conversion to ethyl lactate was achieved. Yields of ethyl lactate around 22.10% were obtained when the lipase was repeatedly used for 5 cycles under the optimal conditions. This indicated that lipase exhibited good stability under the conditions employed. The proper lipase and organic solvent were determined. The results showed that tert-butanol was the best solvent, and the commercial immobilized lipase from candida antarctica (Novozym 435) greatly exceeded all other enzymes using ethanol as an acyl acceptor. Secondly, Plackett-Burman design was applied to evaluate the effects of five parameters (temperature, enzyme concentration, solvent amount, substrate molar ratio, and reaction time). While temperature, enzyme concentration, and substrate molar ratio (ethanol/ammonium lactate) were found to be the significant factors affecting ethyl lactate formation. The three factors were optimized subsequently using response surface methodology (RSM). The mathematical model for the process was established. The optimum process variables were as follows: temperature 67oC, enzyme concentration 30.00 g/mol, substrate molar ratio30.77: 1, water activity 0.12, tert-butanol 37.14: 1(g/g, based on ammonium lactate), 150 r/min, and maximum yield in 30 h was 37.81%. Finally, Kinetics of lipase-catalyzed esterification of ammonium lactate and ethanol were investigated. The reaction rate could be des