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Characterization of Mucosal Disaccharidases from Human Intestine

Department of Physiological Chemistry, University of Veterinary Medicine Hannover, Hannover D-30559, Germany
Author to whom correspondence should be addressed.
Nutrients 2017, 9(10), 1106;
Received: 9 September 2017 / Revised: 30 September 2017 / Accepted: 7 October 2017 / Published: 10 October 2017
In 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
Keywords: intestinal disaccharidases; enzyme activity; pH profile; thermal activity profile intestinal disaccharidases; enzyme activity; pH profile; thermal activity profile
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Amiri, M.; Naim, H.Y. Characterization of Mucosal Disaccharidases from Human Intestine. Nutrients 2017, 9, 1106.

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