A significant broad substrate specificity, that crosses over the usual beta-lactam derivatives, has been observed with an industrial glutaryl-7-aminocephalosporanic acid acylase (GA). This enzyme possesses significant enantioselective amidase and even esterase activity, with a stereopreference for the S-enantiomer. The easy separation of products from unreacted reagents, possessing different physical-chemical properties, is achieved by solvent extraction, avoiding chromatography or distillation during reaction work-up.

Glutaryl acylases: One-reaction enzymes or versatile enantioselective biocatalysts? / Raimondi, S.; Monti, D.; Pagnoni, Ugo Maria; Riva, S.. - In: ADVANCED SYNTHESIS & CATALYSIS. - ISSN 1615-4150. - 345:6-7(2003), pp. 783-789. [10.1002/adsc.200303013]

Glutaryl acylases: One-reaction enzymes or versatile enantioselective biocatalysts?

S. Raimondi;PAGNONI, Ugo Maria;
2003

Abstract

A significant broad substrate specificity, that crosses over the usual beta-lactam derivatives, has been observed with an industrial glutaryl-7-aminocephalosporanic acid acylase (GA). This enzyme possesses significant enantioselective amidase and even esterase activity, with a stereopreference for the S-enantiomer. The easy separation of products from unreacted reagents, possessing different physical-chemical properties, is achieved by solvent extraction, avoiding chromatography or distillation during reaction work-up.
2003
345
6-7
783
789
Glutaryl acylases: One-reaction enzymes or versatile enantioselective biocatalysts? / Raimondi, S.; Monti, D.; Pagnoni, Ugo Maria; Riva, S.. - In: ADVANCED SYNTHESIS & CATALYSIS. - ISSN 1615-4150. - 345:6-7(2003), pp. 783-789. [10.1002/adsc.200303013]
Raimondi, S.; Monti, D.; Pagnoni, Ugo Maria; Riva, S.
File in questo prodotto:
Non ci sono file associati a questo prodotto.
Pubblicazioni consigliate

Licenza Creative Commons
I metadati presenti in IRIS UNIMORE sono rilasciati con licenza Creative Commons CC0 1.0 Universal, mentre i file delle pubblicazioni sono rilasciati con licenza Attribuzione 4.0 Internazionale (CC BY 4.0), salvo diversa indicazione.
In caso di violazione di copyright, contattare Supporto Iris

Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11380/305231
Citazioni
  • ???jsp.display-item.citation.pmc??? ND
  • Scopus 5
  • ???jsp.display-item.citation.isi??? 5
social impact