The N-terminally- and domain V truncated enzyme GtfB of Lactobacillus reuteri strain 121 is member of the GH70 family. This 4,6-glucanotransferase is active on malto-oligosaccharides and starch, thereby yielding elongated isomalto-/malto-oligosaccharides (IMMO) and isomalto-/malto-polymers (IMMPs). The conversion of maltoheptaose (DP 7) using the GtfB-ΔN-ΔV ends up in linear products with a DP > 35,  containing 85 % α(1→4) and 15 % α(1→6) glycosidic linkages. The starch products formed by the GtfB enzyme are derived soluble dietary fibers, which are potentially useful in the food industry.

This product is sold for research use only.
*Activity was measured by following the release of fructose from sucrose. One unit of enzyme activity is defined as the release of 1 μmol of fructose per minute.