Kinetic resolution of DL-phenylalanine methyl ester was carried out using drimobilized α -chymotrypsin (IC) as catalyst. The effects of temperatUre, pH, concentration of substrate and reactionvessels on the resolutio...Kinetic resolution of DL-phenylalanine methyl ester was carried out using drimobilized α -chymotrypsin (IC) as catalyst. The effects of temperatUre, pH, concentration of substrate and reactionvessels on the resolution were investigated. High quality L-phenylalanine was obtained in good yieldby an IC column.展开更多
With recent development of enzyme engineering, the use of enzyme in organic solvents is rapidly increasing. The remarkable stereoselectivity and regioselectivity of reaction catalyzed by enzyme were used to resolve ma...With recent development of enzyme engineering, the use of enzyme in organic solvents is rapidly increasing. The remarkable stereoselectivity and regioselectivity of reaction catalyzed by enzyme were used to resolve many racemic alcohols and esters. A number of results have also been reported about the resolution of amino acids in organic solvents. For example, DL-phenylalanine methyl ester was resolved by α-chymotrypsin in toluene/water biphasic system; in fact, this reaction was carried, out in water;transesterification of DL-phenylalanine propyl ester and methanol was catalyzed by α-chymotrypsin in methanol, and the enzyme used was dissolved in water and the展开更多
The method of preparing D-phenylalanine by asymmetric transformation is reported. D-phenylalanine was prepared from DL-phenylalanine by two-step reaction. D-phenylalanine (2S, 3S)-tartrate was prepared by heating DL-p...The method of preparing D-phenylalanine by asymmetric transformation is reported. D-phenylalanine was prepared from DL-phenylalanine by two-step reaction. D-phenylalanine (2S, 3S)-tartrate was prepared by heating DL-phenylalanine, salicylaldehyde, and (2S, 3S)-tartaric acid in propionic acid; the obtained D-phenylalanine (2S, 3S)-tartrate was treated with triethylamine in ethanol giving D-phenylalanine with 98% optical purity in 69% yield.展开更多
文摘Kinetic resolution of DL-phenylalanine methyl ester was carried out using drimobilized α -chymotrypsin (IC) as catalyst. The effects of temperatUre, pH, concentration of substrate and reactionvessels on the resolution were investigated. High quality L-phenylalanine was obtained in good yieldby an IC column.
文摘With recent development of enzyme engineering, the use of enzyme in organic solvents is rapidly increasing. The remarkable stereoselectivity and regioselectivity of reaction catalyzed by enzyme were used to resolve many racemic alcohols and esters. A number of results have also been reported about the resolution of amino acids in organic solvents. For example, DL-phenylalanine methyl ester was resolved by α-chymotrypsin in toluene/water biphasic system; in fact, this reaction was carried, out in water;transesterification of DL-phenylalanine propyl ester and methanol was catalyzed by α-chymotrypsin in methanol, and the enzyme used was dissolved in water and the
文摘The method of preparing D-phenylalanine by asymmetric transformation is reported. D-phenylalanine was prepared from DL-phenylalanine by two-step reaction. D-phenylalanine (2S, 3S)-tartrate was prepared by heating DL-phenylalanine, salicylaldehyde, and (2S, 3S)-tartaric acid in propionic acid; the obtained D-phenylalanine (2S, 3S)-tartrate was treated with triethylamine in ethanol giving D-phenylalanine with 98% optical purity in 69% yield.
