Journal
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
Volume 64, Issue 33, Pages 6487-6494Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acs.jafc.6b01816
Keywords
alpha-glucosidases; carbohydrate digestion; disaccharides; glycemic; slowly digestible carbohydrates
Funding
- Basic Science Research Program through the National Research Foundation of Korea (NRF) - Ministry of Science, ICT & Future Planning [NRF-2015R1C1A1A02036467]
- U.S. Department of Agriculture (USDA) Agriculture and Food Research Initiative [08-555-03-18793]
- Whistler Center for Carbohydrate Research at Purdue University, West Lafayette, IN, USA
- Canadian Institutes for Health Research
- USDA, Agricultural Research Service [58-6250-1-003]
- Baylor College of Medicine
- Natural Science and Engineering Research Council
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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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