Enzymatic production and characterization of konjac glucomannan oligosaccharides.

Enzymes from a balanced human gut flora are promising tools to design prebiotic oligosaccharides. In this study, we investigated the action of enzymes from fecal bacteria on the complex polysaccharide konjac glucomannan (KGM). The oligosaccharides produced were compared to oligosaccharides from KGM digests with fungal endo-β-(1,4)-glucanase (EG) or endo-β-(1,4)-mannanase (EM). For this purpose, the oligosaccharides from the different digests were first studied for their structural characteristics like monosugar composition and exo-enzymatic degradability, as monitored by capillary electrophoresis with laser-induced fluorescence detection. Whereas the oligosaccharides produced by EG and EM were characteristic for the selectivity of the respective enzyme in cleaving the mannose-/glucose-sugar linkages of KGM, oligosaccharides produced by the fecal enzymes did not point to a sugar-selective degradation. The oligosaccharide fragments from the different digests indicated the KGM polysaccharide to be composed of a backbone composed of short mannose and glucose sequences, to which branches rich in mannose are attached.