Enzymatic synthesis of 3-aminopropyl-1-O-β-Dgalactopyranoside catalyzed by Aspergillus oryzae β-galactosidase

ENZIMAS

GALACTOSIDASAS

GLICOSIDASAS

BIBLIOGRAFIA NACIONAL QUIMICA

2015

Glycosidases represent excellent green chemistry alternatives as catalysts for the synthesis of glycosides, and in particular their stereoselectivity allows the production of anomerically pure glycosides, in only one reaction step using mild reaction conditions. Here, we report the enzymatic synthesis and structural characterization of 3-aminopropyl-1-O-β-D-galactopyranoside. Optimal reaction conditions for the transgalactosylation reaction were 100 mM lactose, 500 mM 3-amino-1-propanol and 24 h of incubation at 50 °C with 6 U/mL of β-galactosidase from Aspergillus oryzae. The fact that the synthesis of 1-propyl-2-O-β-D-galactopyranoside using 1-amino-2-propanol as acceptor was not achieved, and that N-glycoside formation was not observed, confirms the selectivity of β-galactosidase for the synthesis of O-glycosides, and particularly for primary alcohols. The synthesized galactosides were evaluated for their ability to interact with bovine spleen galectin-1 (Gal-1) by using the hemagglutination inhibition assay; results demonstrated that 3-aminopropyl-1-O-β-D-galactopyranoside may be considered as a functionalized galactose moiety more than an efficient Gal-1 inhibitor. The proposed approach constitutes a promising tool for the generation of glycopolymers and glyconanoparticles with potential applications in the development of biosensors as well as construction blocks in chemical synthesis.

Biocatalysis and Biotransformation v. 33, no. 4, 2015. -- p. 197-207

Taylor Francis

2015

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Inglés

Artículo

DOI: 10.3109/10242422.2015.1095678

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