INVESTIGADORES
BRECCIA Javier Dario
artículos
Título:
Transglycosylation specificity of Acremonium sp. alfa-rhamnosyl-beta-glucosidase
Autor/es:
MAZZAFERRO LS; PINUEL L; ERRA-BALSELLS R; GIUDICESSI SL; BRECCIA JD
Revista:
CARBOHYDRATE RESEARCH
Editorial:
ELSEVIER SCI LTD
Referencias:
Año: 2012 vol. 347 p. 69 - 75
ISSN:
0008-6215
Resumen:
Transglycosylation potential of the fungal diglycosidase a-rhamnosyl-b-glucosidase was explored. The biocatalyst was shown to have broad acceptor specificity toward aliphatic and aromatic alcohols. This feature allowed the synthesis of the diglycoconjugated fluorogenic substrate 4-methylumbelliferyl-rutinoside. The synthesis was performed in one step from the corresponding aglycone, 4-methylumbelliferone, and hesperidin as rutinose donor. 4-Methylumbelliferyl-rutinoside was produced in an agitated reactor using the immobilized biocatalyst with a 16% yield regarding the sugar acceptor. The compound was purified by solvent extraction and silica gel chromatography. MALDI-TOF/TOF data recorded for the [M+Na]+ ions correlated with the theoretical monoisotopic mass (calcd [M+Na]+: 507.44 m/z; obs. [M+Na]+: 507.465 m/z). 4-Methylumbelliferyl-rutinoside differs from 4-methylumbelliferyl-glucoside in the rhamnosyl substitution at the C-6 of glucose, and this property brings about the possibility to explore in nature the occurrence of endo-b-glucosidases by zymographic analysis.