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Enantioselective Esterification of Ibuprofen by a Novel Thermophilic Biocatalyst: APE1547
Zhao Dan-tong,Xun Er-na,Wang Jia-xin,Wang Ren,Wei Xiao-fei,Wang Lei,Wang Zhi 한국생물공학회 2011 Biotechnology and Bioprocess Engineering Vol.16 No.4
The enantioselective esterification of ibuprofen catalyzed by a novel thermophilic esterase (APE1547)from the archaeon Aeropyrum pernix K1 was successfully conducted in organic solvents. The effects of acyl acceptor,substrate ratio, organic solvent, temperature, and water activity were investigated. Under optimum conditions, the highest enantioselectivity (E = 38.1) was obtained with a higher enzyme activity (216.5 μmol/g/h). Celites were added into the reaction mixture to remove the water produced in the esterification. The reaction achieved its equilibrium in approximately 96 h with a conversion of 57 and 99%(ee) of the un-reacted (S)-ibuprofen obtained.
Rui Tian,Chun-Hua Yang,Xiao-Fei Wei,Er-Na Xun,Ren Wang,Shu-Gui Cao,Zhi Wang,Lei Wang 한국생물공학회 2011 Biotechnology and Bioprocess Engineering Vol.16 No.2
Aeropyrum pernix esterase (APE1547) was successfully used to catalyze the enantioselective transesterification of (R/S)-2-methyl-1-butanol in an ionic liquid (IL). Effects of various reaction conditions on the synthetic activity of the enzyme as well as enantioselectivity, including the type of IL, acyl donor, temperature, water activity,and substrate molar ratio were inverstigated. APE1547showed good catalytic performance (activity > 0.8 μmol/min/mg, E > 25), and the enzyme-IL mixture was recycled five times with only a slight decrease in catalytic performance.