345643-03-0Relevant academic research and scientific papers
Enantioselective acylation of α-aminonitriles catalysed by Candida antarctica lipase. An unexpected turnover-related racemisation
Lopez-Serrano,Jongejan,Van Rantwijk,Sheldon
, p. 219 - 228 (2001)
Candida antarctica lipase B (Novozyme 435) catalysed the enantioselective acylation of 2-amino-2-phenylacetonitrile 1 with ethyl phenylacetate affording a near enantiopure product in 47% yield. Acylation of 1 and 2-amino-4-phenylbutyronitrile with ethyl a
Resolution of (RS)-phenylglycinonitrile by penicillin acylase-catalyzed acylation in aqueous medium
Chilov, Ghermes G.,Moody, Harold M.,Boesten, Wilhelmus H. J.,Svedas, Vytas K.
, p. 2613 - 2617 (2007/10/03)
A new strategy for the biocatalytic resolution of (R,S)-phenylglycinonitrile, a crucial intermediate in the antibiotic industry, has been developed. While former techniques exploit nitrilases or combinations of nitrile hydratases and amidases, manipulating with nitrile functionality, the current approach is based on a highly efficient and enantioselective acylation of the α-amino group with phenylacetic acid catalyzed by a well known enzyme, penicillin acylase from E. coli, in slightly acidic aqueous medium. It is shown that since the condensation product is poorly soluble, removal of (S)-phenylglycinonitrile from the reaction sphere is almost complete and irreversible, favoring kinetics of the process and making high conversion possible. The proposed approach is characterized by high space-time yield and extends the scope of enzymatic synthesis in aqueous medium.
