Maltase Has Most Versatile alpha-Hydrolytic Activity Among the Mucosal alpha-Glucosidases of the Small Intestine
- Authors
- Lee, Byung-Hoo; Hamaker, Bruce R.
- Issue Date
- Jun-2018
- Publisher
- LIPPINCOTT WILLIAMS & WILKINS
- Keywords
- disaccharides; glucose generation; alpha-glucosidases; alpha-linkages; maltase
- Citation
- JOURNAL OF PEDIATRIC GASTROENTEROLOGY AND NUTRITION, v.66, pp.S7 - S10
- Journal Title
- JOURNAL OF PEDIATRIC GASTROENTEROLOGY AND NUTRITION
- Volume
- 66
- Start Page
- S7
- End Page
- S10
- URI
- https://scholarworks.bwise.kr/gachon/handle/2020.sw.gachon/3734
- DOI
- 10.1097/MPG.0000000000001954
- ISSN
- 0277-2116
- Abstract
- Complete digestion of the glycemic carbohydrates to glucose takes place through the combined action of the 4 mucosal alpha-glucosidases (maltaseglucoamylase and sucrase-isomaltase) in the small intestine. Maltase digests alpha-1,2-and alpha-1,3-disaccharides better than the other alpha-glucosidases, and has, as well, the capability to effectively hydrolyze alpha-1,4 and alpha-1,6 linkages that form the major backbone of a starch molecule. This broad hydrolytic activity on alpha-linkages makes it an enzyme that has the most versatile alpha-hydrolytic activity among the 4 mucosal alpha-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 alpha-1,4 linkages, for modulating the postprandial glycemic response. In addition, using mammalian mucosal alpha-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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