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Intestinal disaccharidases are a group of glycoside hydrolase enzymes anchored to the brush border membrane of the small intestine's microvilli [1, 8]. This enzymatic machinery, which includes sucrase-isomaltase, maltase-glucoamylase, lactase-phlorizin hydrolase, and trehalase, performs the terminal step of carbohydrate digestion by breaking down disaccharides and oligosaccharides into absorbable monosaccharides like glucose, fructose, and galactose [11, 13]. These enzymes are vital for nutrient absorption and the regulation of postprandial blood glucose levels [12, 17]. In clinical practice, they serve as primary therapeutic targets for alpha-glucosidase inhibitors such as acarbose and miglitol, which are used to manage type 2 diabetes by slowing the rate of glucose entry into the bloodstream [4, 6]. Deficiencies in these enzymes, whether congenital or acquired, result in malabsorption syndromes characterized by osmotic diarrhea, bloating, and flatulence due to the colonic fermentation of undigested sugars [18, 20]. Therapeutic strategies for such deficiencies include dietary restriction and enzyme replacement therapies, such as sacrosidase for sucrase deficiency or lactase supplements for lactose intolerance [18, 20].
Competitive inhibition of alpha-glucosidase enzymes to delay carbohydrate digestion and glucose absorption; Enzyme replacement therapy to restore hydrolytic activity in deficient states [4, 18].
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