1007894-89-4Relevant academic research and scientific papers
Chemical modification of lipase for rational enhancement of enantioselectivity
Ema, Tadashi,Inoue, Hiroki
, p. 1374 - 1376 (2015)
Chemical modifications of the I287C mutant of a Burkholderia cepacia lipase afforded various I287C-X conjugates, among which I287C-PAA bearing an N-phenylacetamide (PAA) moiety showed excellent enantioselectivity and catalytic activity for secondary alcohols. Site-directed chemical modifications are powerful tools to control enantioselective biocatalysis.
Screening of liver acetone powders in the resolution of 1-phenylethanols and 1-phenylpropanols derivatives
Solis, Aida,Garcia, Susana,Perez, Herminia I.,Manjarrez, Norberto,Luna, Hector
, p. 549 - 553 (2008/09/20)
Hydrolases from the liver acetone powders (LAPs) of bovine, cat, chicken, turkey, lamb, pig, rabbit, and rat were assessed for the enantioselective hydrolysis of acetates of 1-(4-chlorophenyl)ethanol, 1-(3-bromophenyl)ethanol, 1-(4-chlorophenyl)propanol, 1-(4-bromophenyl)propanol, and 1-(3-bromophenyl)propanol. The enantioselectivity of the hydrolytic reaction was dependent upon the liver hydrolase, substrate, pH of the reaction media, and the cosolvent. The most ester selective LAP was from chicken, and the resulting alcohols had the highest ee (80% to >99%). All of the LAPs tested catalyzed the hydrolysis of 1-(4-chlorophenyl)ethanol, except for lamb LAP.
