Maltase Has Most Versatile α-Hydrolytic Activity Among the Mucosal α-Glucosidases of the Small Intestine

Journal of Pediatric Gastroenterology and Nutrition
Byung-Hoo Lee, Bruce R Hamaker

Abstract

Complete digestion of the glycemic carbohydrates to glucose takes place through the combined action of the 4 mucosal α-glucosidases (maltase-glucoamylase and sucrase-isomaltase) in the small intestine. Maltase digests α-1,2- and α-1,3-disaccharides better than the other α-glucosidases, and has, as well, the capability to effectively hydrolyze α-1,4 and α-1,6 linkages that form the major backbone of a starch molecule. This broad hydrolytic activity on α-linkages makes it an enzyme that has the most versatile α-hydrolytic activity among the 4mucosal α-glucosidases. The slowly digestible properties of the unusual linkages from this research suggest the development of new glycemic oligosaccharides which will be hydrolyzed slowly, compared to α-1,4 linkages, for modulating the postprandial glycemic response. In addition, using mammalian mucosal α-glucosidases is a better fit to characterize carbohydrate digestion properties, compared to fungal amyloglucosidase which is currently applied in in vitro assays.

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Sep 19, 2012·The Journal of Biological Chemistry·Amy Hui-Mei LinBruce R Hamaker
Nov 1, 2012·Journal of Pediatric Gastroenterology and Nutrition·Bruce R HamakerRoberto Quezada-Calvillo
Aug 3, 2016·Journal of Agricultural and Food Chemistry·Byung-Hoo LeeBruce R Hamaker

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Citations

Jul 15, 2020·Bioscience, Biotechnology, and Biochemistry·Ying QiaoKiyoshi Yasukawa

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