Study On Optical Resolute Chiral Glycidyl Butyrate By Enzyme

It is based on the theory of lipase catalyzed enantioselective hydrolysis. In this paper, efficient resolution of a racemic glycidyl butyrate was achieved by Porcine Pancreatic Lipase(PPL) catalyzed hydrolyzation. The technological conditions to resolute glycidyl butyrate by enzyme in water phase and organic solvent have been studied gropingly And Optimized by Response Surface Methodology(RSM) in bufferis; In order to use lipase economically.The immobilization about PPL have been studied. The comparison of the character about immobilized enzyme by Nano- SiO2 with sodium alginate was performed; The effect of the conditions about immobilizing lipase using Nano- SiO2 on its activity have been achieved; The cheracteristics of the immobilized enzyme have been studied; In order to use the immobilized lipase,the conditions of catalyzed hydrolyzation by it were optimized by combination single factor design and orthogonal test design.The result showed that in bufferis, The optimum initial pH of buffer is7.5. The optimum lipase concentration is about 30mg/(g butyrate). The optimum initial substrate concentration is around 0.4mol/l.The optimum temperature for the reaction is around 30℃. The optimum shaking speed is about 150r/min.The optimum reaction time is about 4h. Under the condition, we achieved the optical purity of the finally recovered (R)-glycidyl butyrate and the ee% was about 85%, the substrate conversion efficiency is about 51.78%.After the optimization by RSM, the optimum condition is: substrate concentration 0.499mol/l; lipase concentration of 30.2mg/g; a temperature of 29.7℃; pH 7.6; reaction time of 4h; shaking speed at 150r/min.The ee% has been 93.28%.The optimum condition of Lipase-catalyzed kinetic resolution of racemic glycidyl butyrate in organic solvents is organic solvents of cyclohexane; water content of 6%;pH7.8; substrate concentration of 0.7mol/l.The result of the experimentation about Immobilize lipase is : The immobilized PPL using Nano- SiO2 as carrier by adsorption is better than the lipase immobilizedwith sodium alginate carrier. The results of the immobilization of PPL using Nano-SiO2 as carrier showed that the maximum activity of immobilized lipase was obtained when the aqueous silicon sols was blended with the solution of lipase as 1:2 at 30℃.The aqueous silicon sols was gained by whipping 2h at pH7.5 and the solid:liquid aspect ratio of l:25.The specific activity of immobilized lipase is 19.67U/g and the recovery rate of the lipase is 82.9% while that of the lipase immobilized with sodium alginate carrier is 54.25%. The catalyzed hydrolysis of olive oil by immobilized lipase on nano- SiO2 as carrier had been studied.The result of experimentation is:The activity of immobilized lipase is the highest at 50℃and pH8.2;Its heat stability and storage stability is improved by immobilization; The apparent Km of immobilized lipase is 0.37x 102g/L while Km of protoenzyme is 1.01X02g/l;The immobilized lipase has good reusabilities activity still can reserve 59.7% when it was used to catalyze hydrolysis of olive oil. The optimum conditions about hydrolization glycidyl butyrate by the immobilized enzyme as following: a temperature of 30℃,pH7.8, substrate concentration and lipase dosage of 0.4mol/l and 0.32g,and shaking speed of 200r/min,reaction time of 4h.