Inhibition of human digestive enzymes by hydrogenated malto-oligosaccharides
Würsch, P.; Del Vedovo, S.
International Journal for Vitamin and Nutrition Research. Internationale Zeitschrift für Vitamin- und Ernahrungsforschung. Journal International de Vitaminologie et de Nutrition 51(2): 161-165
1981
ISSN/ISBN: 0300-9831 PMID: 6169675 Document Number: 173716
Maltose, malto-oligosaccharides and their reduced sugar analogues were tested as substrates and inhibitors of human salivary alpha -amylase and small intestine beta -glucosidases. Maltotriose and maltotetraose as well as their reduced analogues inhibited alpha -amylase competitively. Maltitol, maltotriitol and maltotetraitol were not hydrolysed. The small intestine maltases hydrolysed maltitol at low rate, but maltotriitol was split almost at the same rate as maltrotriose. Those 3 sugars were weak mutual inhibitors. Glucoamylase in the small intestine was slightly inhibited by maltotriitol but not by maltitol whereas fungal glucoamylase activity was strongly competitively inhibited by maltitol. Where the reducing end glucose unit of the malto-oligosaccharides below 5 glucose units are converted into sorbitol, their inhibitory effect is retained but their capacity of hydrolysis is reduced or disappears.