Enantioselective esterase activity of an industrial glutaryl acylase (Articolo in rivista)

Type
Label
  • Enantioselective esterase activity of an industrial glutaryl acylase (Articolo in rivista) (literal)
Anno
  • 2005-01-01T00:00:00+01:00 (literal)
Alternative label
  • Adani S., Raimondi S., Forti L., Monti D., Riva S. (2005)
    Enantioselective esterase activity of an industrial glutaryl acylase
    in Tetrahedron: asymmetry (Print)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Adani S., Raimondi S., Forti L., Monti D., Riva S. (literal)
Pagina inizio
  • 2509 (literal)
Pagina fine
  • 2513 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 16 (literal)
Rivista
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • Istituto di Chimica del Riconoscimento Molecolare (ICRM), C.N.R., Via Mario Bianco 9, 20131 Milano, Italy. Dipartimento di Chimica, Universita` di Modena & Reggio Emilia, Via Campi 183, 41100 Modena, Italy (literal)
Titolo
  • Enantioselective esterase activity of an industrial glutaryl acylase (literal)
Abstract
  • The unexpected esterase activity of an industrial glutaryl acylase was investigated. Glutaryl esters of a series of primary and secondary alcohols as well as of phenols were all efficiently hydrolyzed, the only exception being the sterically hindered glutarate of thymol. The enantioselectivities of the acylase, which were evaluated with three of these substrates, were quite low (E values ranging between 1.9 and 7.2), but were significantly improved by substrate and/or solvent engineering. Enantiomerically enriched hydrolyzed alcohols and unreacted glutarates can be easily separated by selective extraction, thus avoiding chromatographic steps. (literal)
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