β-Glucosidase from an extreme thermophile,
Thermus sp. Z-1, has a wide substrate specificity and a strong β-galactosidase activity.
1H-NMR analysis was performed on the structure of oligosaccharides produced in the presence of the enzyme by a transglycosilation reaction, during hydrolysis of lactose, at a high temperature. Oligosaccharides were prepared from a 0.88 M lactose solution by reacting with β-glucosidase from
Thermus sp. Z-1 at the concentration of 1.4 U/m
l at 70℃ for 120 min.
Newly transgalactosylated oligosaccharides containing disaccharides and trisaccharides in the reaction mixture were isolated by gel filtration chromatography (Bio Gel P-2) and preparative paper chromatography (PPC), followed by an analysis with
1H-NMR.
In trisaccharides, the major component was Galβ1→3Galβ1→4Glc (3'-GL) and Galβ1→6Galβ1→4Glc (6'-GL) and another oligosaccharides were also determined by
1H-NMR.
These results suggested that the β-glucosidase from
Thermus sp. Z-1 was characterized, preferably by the transfer of galactosyl residue at the non-reducing end by β1→3 linkage.
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