26395-99-3Relevant articles and documents
On the substrate preference of glutaryl acylases
Rosini, Elena,Monelli, Claudia Stella,Pollegioni, Loredano,Riva, Sergio,Monti, Daniela
experimental part, p. 52 - 58 (2012/04/11)
The substrate preferences of three acylases - two wild-type enzymes and an evolved variant obtained by directed evolution - which are prototypical enzymes for glutaryl-7-ACA acylase and cephalosporin C acylase subfamilies, have been investigated. A preliminary screening of enzymes' performances on a large set of substrates has been carried out by a colorimetric assay performed in 96-well plates and by a pH-Stat monitoring the hydrolytic activities. Subsequently, kinetic data for selected substrates have been determined, thus elucidating the substrate preference of members of glutaryl-7-ACA acylase vs. cephalosporin C acylase subfamilies. These achievements pave the way to the ability of choosing the best enzyme for the hydrolysis of different compounds of industrial importance.
The multilayer polymer film
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, (2007/10/09)
The use of multilayer film structure comprising at least two unfilled layers of polymeric material substantially devoid of opacifying agent and at least two filled layers of polymeric material wherein said filled layers comprise at least 5% by weight of o
Glutaryl Acylases: One-Reaction Enzymes or Versatile Enantioselective Biocatalysts?
Raimondi, Stefano,Monti, Daniela,Pagnoni, Ugo Maria,Riva, Sergio
, p. 783 - 789 (2007/10/03)
A significant broad substrate specificity, that crosses over the usual β-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.