Würsch P, Del Vedovo S
Int J Vitam Nutr Res. 1981;51(2):161-5.
Maltose, malto-oligosaccharides and their reduced sugar analogues have been tested as substrates and inhibitors of human salivary alpha-amylase and small intestine alpha-glucosidases. - Maltotriose and maltotetraose as well as their reduced analogues inhibited competitively alpha-amylase. Maltitol, maltotriitol and maltotetraitol were not hydrolyzed. - The small intestine maltases hydrolyzed maltitol at a very low rate, but maltotriitol was split almost at the same rate as maltotriose. These three sugars were weak mutual inhibitors. - The small intestine glucoamylase was slightly inhibited by maltotriitol but not by maltitol whereas fungal glucoamylase activity was strongly competitively inhibited by maltitol. This study shows that where the reducing end glucose unit of the malto-oligosaccharides below five glucose units are converted into sorbitol, their inhibitory effect is retained but their capacity of hydrolysis is reduced or disappears.
麦芽糖、麦芽低聚糖及其还原糖类似物已被作为人唾液α-淀粉酶和小肠α-葡萄糖苷酶的底物和抑制剂进行了测试。- 麦芽三糖和麦芽四糖及其还原类似物竞争性抑制α-淀粉酶。麦芽糖醇、麦芽三糖醇和麦芽四糖醇不被水解。- 小肠麦芽糖酶以非常低的速率水解麦芽糖醇，但麦芽三糖醇的分解速率几乎与麦芽三糖相同。这三种糖是弱相互抑制剂。- 小肠葡糖淀粉酶受到麦芽三糖醇的轻微抑制，但不受麦芽糖醇抑制，而真菌葡糖淀粉酶活性受到麦芽糖醇的强烈竞争性抑制。本研究表明，低于五个葡萄糖单位的麦芽低聚糖的还原端葡萄糖单元转化为山梨醇时，其抑制作用得以保留，但水解能力降低或消失。
