Enzymatic catalysis by lipase from Candida cylindracea: enantiomeric activity evaluation by 1H and 13C NMR.
Lipolytic enzymes represent an important class of biocatalysts and are widely used in the resolution of racemic mixtures. The activity of lipase from Candida cylindracea at different temperatures has been studied by NMR determination of the enantiomeric excess in the enantioselective hydrolysis of 2-arylpropionic acid esters of pharmacological interest. At a purpose, a system based on Europium (III) chiral shift reagent has been settled and utilized.
Cernia
E
E
Department of Chemistry, University La Sapienza of Rome, Italy.
Delfini
M
M
Magri
A D
AD
Palocci
C
C
D002175:Candida / Q000201:enzymology*; D002384:Catalysis; D008049:Lipase / Q000737:chemistry / Q000378:metabolism*; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D013237:Stereoisomerism; D013696:Temperature
D008049:Lipase