2. Academic Validation
  3. Contribution of the Individual Small Intestinal α-Glucosidases to Digestion of Unusual α-Linked Glycemic Disaccharides

Contribution of the Individual Small Intestinal α-Glucosidases to Digestion of Unusual α-Linked Glycemic Disaccharides

  • J Agric Food Chem. 2016 Aug 24;64(33):6487-94. doi: 10.1021/acs.jafc.6b01816.
Byung-Hoo Lee 1 2,  David R Rose 3,  Amy Hui-Mei Lin 2 4,  Roberto Quezada-Calvillo 5,  Buford L Nichols 6,  Bruce R Hamaker 2 7
Affiliations

Affiliations

  • 1 Department of Food Science & Biotechnology, College of BioNano Technology, Gachon University , Seongnam, Gyeonggi-do 13120, Republic of Korea.
  • 2 Whistler Center for Carbohydrate Research, Department of Food Science, Purdue University , West Lafayette, Indiana 47907, United States.
  • 3 Department of Biology, University of Waterloo , Waterloo, Ontario N2L 3G1, Canada.
  • 4 Bi-State School of Food Science, University of Idaho and Washington State University , Moscow, Idaho 83844, United States.
  • 5 Department of Chemistry, Universidad Autonoma de San Luis Potosi , San Luis Potosi 78360, Mexico.
  • 6 USDA, Agricultural Research Service, Children's Nutrition Research Center and Department of Pediatrics, Baylor College of Medicine , Houston, Texas 77030, United States.
  • 7 Department of Food Science & Technology, Sejong University , Gunja-Dong, Gwangjin-Gu, Seoul 05006, Republic of Korea.
PMID: 27480812 DOI: 10.1021/acs.jafc.6b01816
Abstract

The mammalian mucosal α-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 α-linkages that are digested to glucose slowly by these enzymes. Here, we look at disaccharides with various possible α-linkages and their hydrolysis. Hydrolytic properties of the maltose and sucrose isomers were determined using rat intestinal and individual recombinant α-glucosidases. The individual α-glucosidases had moderate to low hydrolytic activities on all α-linked disaccharides, except trehalose. Maltase (N-terminal MGAM) showed a higher ability to digest α-1,2 and α-1,3 disaccharides, as well as α-1,4, making it the most versatile in α-hydrolytic activity. These findings apply to the development of new glycemic oligosaccharides based on unusual α-linkages for extended glycemic response. It also emphasizes that mammalian mucosal α-glucosidases must be used in in vitro assessment of digestion of such carbohydrates.

Keywords

carbohydrate digestion; disaccharides; glycemic; slowly digestible carbohydrates; α-glucosidases.

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