Autor: |
Alatorre-Santamaría, Sergio, Escamilla-Lozano, Yolanda, Guzmán-Rodríguez, Francisco, García-Garibay, Mariano, Rodríguez-Serrano, Gabriela, Gómez-Ruiz, Lorena, Cruz-Guerrero, Alma |
Zdroj: |
Applied Biochemistry & Biotechnology; Jun2019, Vol. 188 Issue 2, p369-380, 12p |
Abstrakt: |
Glycosylhydrolases of various origins were used to produce fucose-containing disaccharides with prebiotic potential using different donor substrates and l-fucose as the acceptor substrate. Eight different disaccharides were synthesized as follows: three β-d-galactosyl-l-fucosides with glycosidase CloneZyme Gly-001-02 using d-lactose as a donor substrate, two with a structure similar to prebiotics; one β-d-galactosyl-l-fucose with β-d-galactosidase from Aspergillus oryzae using d-lactose as a substrate donor; and four α-d-glucosyl-l-fucosides with α-d-glucosidase from Saccharomyces cerevisiae using d-maltose as a donor substrate. All disaccharides were purified and hydrolyzed. In all cases, an l-fucose moiety was present, and it was confirmed for β-d-galactosyl-l-fucose by mass spectrometry. High concentrations of l-fucose as the acceptor substrate enhanced the synthesis of the oligosaccharides in all cases. The three enzymes were able to synthesize fucose-containing disaccharides when l-fucose was used as the acceptor substrate, and the highest yield was 20% using β-d-galactosidase from Aspergillus oryzae. [ABSTRACT FROM AUTHOR] |
Databáze: |
Complementary Index |
Externí odkaz: |
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