Contribution of the Individual Small Intestinal alpha-Glucosidases to Digestion of Unusual alpha-Linked Glycemic Disaccharides
- Authors
- Lee, Byung-Hoo; Rose, David R.; Lin, Amy Hui-Mei; Quezada-Calvillo, Roberto; Nichols, Buford L.; Hamaker, Bruce R.
- Issue Date
- 24-Aug-2016
- Publisher
- AMER CHEMICAL SOC
- Keywords
- alpha-glucosidases; carbohydrate digestion; disaccharides; glycemic; slowly digestible carbohydrates
- Citation
- JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY, v.64, no.33, pp.6487 - 6494
- Journal Title
- JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
- Volume
- 64
- Number
- 33
- Start Page
- 6487
- End Page
- 6494
- URI
- https://scholarworks.bwise.kr/gachon/handle/2020.sw.gachon/7999
- DOI
- 10.1021/acs.jafc.6b01816
- ISSN
- 0021-8561
- Abstract
- The mammalian mucosal alpha-glucosidase complexes, maltase-glucoamylase (MGAM) and sucrase-isomaltase (SI), have two catalytic subunits (N- and C-termini). Concurrent with the desire to modulate glycemic response, there has been a focus on di/oligosaccharides with unusual alpha-linkages that are digested to glucose slowly by these enzymes. Here, we look at disaccharides with various possible alpha-linkages and their hydrolysis. Hydrolytic properties of the maltose and sucrose isomers were determined using rat intestinal and individual recombinant alpha-glucosidases. The individual alpha-glucosidases had moderate to low hydrolytic activities on all alpha-linked disaccharides, except trehalose. Maltase (N-terminal MGAM) showed a higher ability to digest alpha-1,2 and alpha-1,3 disaccharides, as well as alpha-1,4, making it the most versatile in alpha-hydrolytic activity. These findings apply to the development of new glycemic oligosaccharides based on unusual alpha-linkages for extended glycemic response. It also emphasizes that mammalian mucosal alpha-glticosidases must be used in in-vitro assessment of digestion of such carbohydrates.
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