Improving lipase-catalyzed enantioselective ammonolysis of phenylglycine methyl ester in organic solvent by in situ racemization.
Lipase-catalyzed enantioselective ammonolysis of phenylglycine methyl ester was processed by in situ racemization with ammonium carbamate as the acyl acceptor. Using 1 mM benzaldehyde or 0.6 mM chloropyridoxal as the racemizing catalyst, 80% substrate conversion with an enantiomeric excess of the product of 95% were achieved at 20 degrees C after 7 h reaction.
Du
Wei
W
Department of Chemical Engineering, Tsinghua University, 100084 Beijing, PR China. duwei@mail.tsinghua.edu.cn
Zong
Minhua
M
Guo
Yong
Y
Liu
Dehua
D
D000641:Ammonia / Q000737:chemistry; D001547:Benzaldehydes / Q000737:chemistry*; D002219:Carbamates / Q000737:chemistry*; D002384:Catalysis; D005656:Fungal Proteins; D005998:Glycine / Q000031:analogs & derivatives* / Q000138:chemical synthesis / Q000737:chemistry*; D006859:Hydrogen / Q000737:chemistry; D008049:Lipase / Q000737:chemistry*; D011730:Pyridoxal / Q000031:analogs & derivatives* / Q000737:chemistry; D012997:Solvents / Q000737:chemistry; D013237:Stereoisomerism; D013696:Temperature
D001547:Benzaldehydes; D002219:Carbamates; D005656:Fungal Proteins; D012997:Solvents; C033393:methyl phenylglycine; D011730:Pyridoxal; D000641:Ammonia; D006859:Hydrogen; D008049:Lipase; C431349:lipase B, Candida antarctica; C070766:carbamic acid; C032175:benzaldehyde; D005998:Glycine