183811-88-3Relevant articles and documents
Improved synthesis of disaccharides with Escherichia coli β-galactosidase using bio-solvents derived from glycerol
Pérez-Sánchez, María,Cortés Cabrera, álvaro,García-Martín, Héctor,Sinisterra, J. Vicent,García, José I.,Hernáiz, María J.
, p. 7708 - 7712 (2011)
A noticeably increase in activity, keeping total regioselectivity was found in the synthetic behaviour of Escherichia coli β-galactosidase in glycerol-based solvents using a 1:7 molar ratio of donor (pNP-β-Gal): acceptor (GlcNAc). Yields of up to 97% of β(1→6) with different solvents were found. These reactions take place without noticeable hydrolytic activity and with total regioselectivity, representing a considerable improvement over the use of aqueous buffer or conventional organic solvents. There is a clear dependence of the catalytic results on the solvent structure, which is analysed in terms of polarity and hydrophobicity.
Sustainable synthesis of N-acetyllactosamine using an immobilized β-galactosidase on a tailor made porous polymer
Aires-Trapote, Antonio,Tamayo, Aitana,Rubio, Juan,Rumbero, Angel,Hernáiz, María J.
, p. 40375 - 40383 (2015/05/20)
Porous polymer particles containing surface epoxy groups were synthesized for immobilizing β-galactosidase from Bacillus circulans. Enzyme immobilization was achieved by covalent attachment to a custom made porous polymer and the biocatalyst was character
Glycosyl azides - An alternative way to disaccharides
Bojarova, Pavla,Petraskova, Lucie,Ferrandi, Erica Elisa,Monti, Daniela,Pelantova, Helena,Kuzma, Marek,Simerska, Pavla,Kren, Vladimir
, p. 1514 - 1520 (2008/09/17)
Glycosyl azides are shown to be efficient donors for β-galactosidases, β-glucosidases and α mannosidases. Only α-galactosidases do not cleave the respective glycosyl azide 1 and, moreover, they exhibit competitive inhibition (especially α-galactosidase fr