Coupling reactions of trehalose synthase from Pyrococcus horikoshii: cost-effective synthesis and anti-adhesive activity of α-galactosyl oligosaccharides using a one-pot three-enzyme system with trehalose.
Bioresour Technol
; 136: 743-6, 2013 May.
Article
en En
| MEDLINE
| ID: mdl-23545070
ABSTRACT
A new sugar nucleotide cycling (SNC) process was established in a one-pot three enzyme-coupled reaction using disaccharide trehalose. Trehalose synthase from Pyrococcus horikoshii could be applied to the SNC process for the synthesis of functional α-galactosyl oligosaccharides, α-galactose (Gal) epitopes and globotriose, using the effective regeneration of UDP-Gal. The α-Gal epitopes and globotriose were found to attach to the cell-surface of enteropathogenic Escherichia coli O127 (EPEC) which were bound to human Caco-2 cells. These α-galactosyl oligosaccharides were able to prohibit the attachment of EPEC, which could have resulted in colonization and disease. The α-Gal epitope III with a lactulose acceptor showed the most inhibitory activity of anti-adhesion. The results suggest that the α-galactosyl oligosaccharides may be alternative anti-adhesion molecules that overcome antibiotic resistance.
Texto completo:
1
Banco de datos:
MEDLINE
Asunto principal:
Oligosacáridos
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Trehalosa
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Adhesión Bacteriana
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Biotecnología
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Pyrococcus horikoshii
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Glucosiltransferasas
Tipo de estudio:
Health_economic_evaluation
Límite:
Animals
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Humans
Idioma:
En
Año:
2013
Tipo del documento:
Article