beta-1,4-galactosyltransferase-catalyzed glycosylation of sugar derivatives: Modulation of the enzyme activity by alpha-lactalbumin, immobilization and solvent tolerance (Articolo in rivista)

Type

• Articolo in rivista (Classe)
• Prodotto della ricerca (Classe)

Label

• beta-1,4-galactosyltransferase-catalyzed glycosylation of sugar derivatives: Modulation of the enzyme activity by alpha-lactalbumin, immobilization and solvent tolerance (Articolo in rivista) (literal)

Anno

• 2006-01-01T00:00:00+01:00 (literal)

Alternative label

• Pisvejcova A., Rossi C., Husakova L., Kren V., Riva S., Monti D. (2006)
  beta-1,4-galactosyltransferase-catalyzed glycosylation of sugar derivatives: Modulation of the enzyme activity by alpha-lactalbumin, immobilization and solvent tolerance
  in Journal of molecular catalysis. B, Enzymatic (Print)
  (literal)

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

• Pisvejcova A., Rossi C., Husakova L., Kren V., Riva S., Monti D. (literal)

Pagina inizio

• 98 (literal)

Pagina fine

• 104 (literal)

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

• 39 (literal)

Rivista

• Journal of molecular catalysis. B, Enzymatic (Rivista)

Note

• ISI Web of Science (WOS) (literal)

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

• Institute of Microbiology, Academy of Sciences of the Czech Republic, Laboratory of Biotransformation, V?denska 1083, CZ 142 20 Prague 4, Czech Republic. Istituto di Chimica del Riconoscimento Molecolare, CNR, Via Mario Bianco 9, 20131 Milan, Italy (literal)

Titolo

• beta-1,4-galactosyltransferase-catalyzed glycosylation of sugar derivatives: Modulation of the enzyme activity by alpha-lactalbumin, immobilization and solvent tolerance (literal)

Abstract

• The influence of different parameters on the activity of the beta-1,4-galactosyltransferase (beta-1,4-GalT) from bovine milk has been investigated using various acceptor and donor substrates. It was found that the \"specifier\" protein alpha-lactalbumin (alpha-LA), which interacts with beta-1,4-GalT forming the lactose synthase (LS) complex, is not necessary when the acceptors are different glucopyranosides, and, in some cases, it can even have an inhibitory effect, like with the complex glucosides ginsenoside Rg 1 (1) and colchicoside (2). By optimization of the reaction conditions, the galactosylated and glucosylated derivatives of 2 were prepared, using UDP-Gal and UDP-Glc as sugar donors, respectively, and characterized. Moreover, beta-1,4-GalT was covalently immobilized on Eupergit C 250 L in the absence of alpha-LA, and the synthetic performances of this immobilized biocatalyst were evaluated. Finally, the best organic cosolvents to be used both with beta-1,4-GalT and the LS complex were identified. (literal)

Prodotto di

• Istituto di chimica del riconoscimento molecolare (ICRM) (Istituto)
• Applicazioni sintetiche della biocatalisi (PM.P03.009.002) (Modulo)

Autore CNR

• DANIELA MONTI (Unità di personale interno)
• SERGIO RIVA (Unità di personale interno)

Incoming links:

Autore CNR di

• SERGIO RIVA (Unità di personale interno)
• DANIELA MONTI (Unità di personale interno)

Prodotto

• Istituto di chimica del riconoscimento molecolare (ICRM) (Istituto)
• Applicazioni sintetiche della biocatalisi (PM.P03.009.002) (Modulo)

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

• Journal of molecular catalysis. B, Enzymatic (Rivista)