The GtfC enzyme of Exiguobacterium sibiricum 255-15 is a member of the GH70 family. This glucanotransferase is active on malto-oligosaccharides and starch, synthesizing isomalto/malto-oligosaccharides (IMMOs) containing 52 % α(1→6) and 35 % α(1→4)-glycosidic linkages using amylose V. Biochemically, GtfC enzymes are close related to the GH70 GtfB enzymes. Although its domain organization is more closely related to GH13 enzymes (α-amylases). Making the GtfC 4,6-glucanotransferase an interesting intermediate between α-amylase and glucansucrase enzymes.

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*Enzyme activity was determined by the iodine-staining assay using amylose as substrate. One unit of activity is defined as the amount of enzyme preparation converting 1 mg of substrate per min.