Autor: |
Fourage, L., Colas, B. |
Předmět: |
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Zdroj: |
Applied Microbiology & Biotechnology; Aug2001, Vol. 56 Issue 3/4, p406-410, 5p, 3 Charts, 2 Graphs |
Abstrakt: |
The thermostable β-glycosidase from Thermus thermophilus, cloned and overexpressed in Escherichia coli was used to catalyze the transfer of β-D-glucosyl and β-D-fucosyl from the corresponding p-nitrophenyl-β-D-glycopyranosides to a hydroxyl group of glucose in the synthesis of β-D-glucosyl-D-glucopyranoses and β-D-fucosyl-D-glucopyranoses. The yields in disaccharides produced under conditions of non-initial velocity were very attractive and the formation of the β(1–3) linked disaccharides was largely favored. The enzyme could constitute a valuable biocatalyst for the synthesis of disaccharides involving such structures as, for example, Bifidus factors. [ABSTRACT FROM AUTHOR] |
Databáze: |
Complementary Index |
Externí odkaz: |
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