High-throughput enzymatic method for enantiomeric excess determination of O-acetylated cyanohydrins.
The reaction yield and enantiomeric excess of O-acetylated cyanohydrin reaction products from a library of chiral catalysts can be analyzed by a three-step screening method. Alcohol dehydrogenase and NADH are used to analyze unreacted substrate. A lipase with absolute specificity converts one enantiomer to a quantifiable product before the remaining enantiomer is hydrolyzed with an unspecific esterase and quantified.
KTH School of Biotechnology, Department of Biochemistry, AlbaNova University Center, SE 106 91 Stockholm, Sweden.
Anders
A
Hamberg
Stina
S
Lundgren
Maël
M
Penhoat
Christina
C
Moberg
Karl
K
Hult
D000107:Acetylation; D000818:Animals; D001547:Benzaldehydes / Q000737:chemistry; D004950:Esterases / Q000737:chemistry*; D005656:Fungal Proteins; D006868:Hydrolysis; D008049:Lipase / Q000737:chemistry*; D008099:Liver / Q000201:enzymology; D009243:NAD / Q000737:chemistry; D009570:Nitriles / Q000032:analysis / Q000737:chemistry*; D013237:Stereoisomerism; D013552:Swine
D001547:Benzaldehydes; D005656:Fungal Proteins; D009570:Nitriles; C430593:cyanohydrin; D009243:NAD; D004950:Esterases; D008049:Lipase; C431349:lipase B, Candida antarctica; C032175:benzaldehyde