The N-terminally- and domain V truncated enzyme GtfB of Lactobacillus reuteri strain 121 is a 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→6) and 15 % α(1→4) glycosidic linkages. The starch products formed by the GtfB enzyme are derived soluble dietary fibers, which are potentially useful in the food industry.

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*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.