http://www.cnr.it/ontology/cnr/individuo/prodotto/ID17795
On the substrate preference of glutaryl acylases (Articolo in rivista)
- Type
- Label
- On the substrate preference of glutaryl acylases (Articolo in rivista) (literal)
- Anno
- 2012-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1016/j.molcatb.2011.12.001 (literal)
- Alternative label
Rosini, Elena; Monelli, Claudia Stella; Pollegioni, Loredano; Riva, Sergio; Monti, Daniela (2012)
On the substrate preference of glutaryl acylases
in Journal of molecular catalysis. B, Enzymatic (Print)
(literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- Rosini, Elena; Monelli, Claudia Stella; Pollegioni, Loredano; Riva, Sergio; Monti, Daniela (literal)
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- ISI Web of Science (WoS) (literal)
- ISI Web of Science (WOS) (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
- University of Insubria; University of Insubria; Consiglio Nazionale delle Ricerche (CNR); Polytechnic University of Milan (literal)
- Titolo
- On the substrate preference of glutaryl acylases (literal)
- Abstract
- 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-Star 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. (C) 2011 Elsevier B.V. All rights reserved. (literal)
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