http://www.cnr.it/ontology/cnr/individuo/prodotto/ID283921

Milnacipran as a challenging example of aminomethyl substrate for lipase-catalyzed kinetic resolution (Articolo in rivista)

Type

Label

Milnacipran as a challenging example of aminomethyl substrate for lipase-catalyzed kinetic resolution (Articolo in rivista) (literal)

Anno

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi

Alternative label

Sanfilippo C.; Nicolosi G.; Patti A. (2014)
Milnacipran as a challenging example of aminomethyl substrate for lipase-catalyzed kinetic resolution
in Journal of molecular catalysis. B, Enzymatic (Print)
(literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori

Pagina inizio

Pagina fine

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#url

http://www.scopus.com/inward/record.url?eid=2-s2.0-84898638292&partnerID=q2rCbXpz (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume

Rivista

Note

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni

Istituto di Chimica Biomolecolare Del CNR, Via Paolo Gaifami 18, Catania, 95126, Italy (literal)

Titolo

Milnacipran as a challenging example of aminomethyl substrate for lipase-catalyzed kinetic resolution (literal)

Abstract

A biocatalysed procedure for the kinetic resolution of milnacipran, (±)-1 was developed and optimized by careful choice of the reaction parameters. The reaction of (±)-1 with methyl iso-butyrate as acyl donor in the presence of Novozyme 435 in tert-butyl methyl ether proceeded with moderate enantioselectivity giving the more pharmacologically active enantiomer of milnacipran (-)-1 as unreacted substrate and the corresponding amide (-)-4 both in optically enriched form. When the enzymatic reaction was prolonged up to 65% substrate conversion enantiopure levomilnacipran (-)-1 (98% ee) was directly recovered from the reaction mixture by simple extraction workup. © 2014 Published by Elsevier B.V. (literal)

Prodotto di