Characterization of Mucosal Disaccharidases from Human Intestine
AbstractIn this study, we used a brush border membrane (BBM) preparation from human small intestine to analyze the proportion and the activity of major intestinal disaccharidases, including sucrase-isomaltase (SI), maltase-glucoamylase (MGAM) and lactase-phlorizin hydrolase (LPH). SI, MGAM and LPH respectively constituted 8.2%, 2.7% and 1.4% of total BBM protein. The activity of SI and LPH decreased threefold after purification from the brush border membrane, which highlights the effect of membrane microdomains on the functional capacity of these enzymes. All of the disaccharidases showed optimal activity at pH 6, over 50% residual activity between pH 5 to pH 7, and increasing activity with rising temperatures up to 45 °C, along with a stable functional structure. Therefore the enzymes can withstand mild intraluminal pH alterations with adequate function, and are able to increase their activity with elevated core body temperature. Our data provide a functional measure for characterization of intestinal disaccharidases under different physiological and pathological conditions. View Full-Text
Share & Cite This Article
Amiri, M.; Naim, H.Y. Characterization of Mucosal Disaccharidases from Human Intestine. Nutrients 2017, 9, 1106.
Amiri M, Naim HY. Characterization of Mucosal Disaccharidases from Human Intestine. Nutrients. 2017; 9(10):1106.Chicago/Turabian Style
Amiri, Mahdi; Naim, Hassan Y. 2017. "Characterization of Mucosal Disaccharidases from Human Intestine." Nutrients 9, no. 10: 1106.
Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.