title: Contribution of the Individual Small Intestinal α-Glucosidases to Digestion of Unusual α-Linked Glycemic Disaccharides.
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.
authors.affiliation: Department of Food Science & Biotechnology, College of BioNano Technology, Gachon University , Seongnam, Gyeonggi-do 13120, Republic of Korea.|Whistler Center for Carbohydrate Research, Department of Food Science, Purdue University , West Lafayette, Indiana 47907, United States.
authors.forename: Byung-Hoo
authors.initials: BH
authors.lastname: Lee
authors.affiliation: Department of Biology, University of Waterloo , Waterloo, Ontario N2L 3G1, Canada.
authors.forename: David R
authors.initials: DR
authors.lastname: Rose
authors.affiliation: Whistler Center for Carbohydrate Research, Department of Food Science, Purdue University , West Lafayette, Indiana 47907, United States.|Bi-State School of Food Science, University of Idaho and Washington State University , Moscow, Idaho 83844, United States.
authors.forename: Amy Hui-Mei
authors.initials: AH
authors.lastname: Lin
authors.affiliation: Department of Chemistry, Universidad Autonoma de San Luis Potosi , San Luis Potosi 78360, Mexico.
authors.forename: Roberto
authors.initials: R
authors.lastname: Quezada-Calvillo
authors.affiliation: USDA, Agricultural Research Service, Children's Nutrition Research Center and Department of Pediatrics, Baylor College of Medicine , Houston, Texas 77030, United States.
authors.forename: Buford L
authors.initials: BL
authors.lastname: Nichols
authors.affiliation: Whistler Center for Carbohydrate Research, Department of Food Science, Purdue University , West Lafayette, Indiana 47907, United States.|Department of Food Science & Technology, Sejong University , Gunja-Dong, Gwangjin-Gu, Seoul 05006, Republic of Korea.
authors.forename: Bruce R
authors.initials: BR
authors.lastname: Hamaker
mesh_terms: D000818:Animals; D004063:Digestion; D004187:Disaccharides / Q000737:chemistry*; D005947:Glucose / Q000737:chemistry; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D007421:Intestine, Small / Q000201:enzymology*; D008320:Maltose / Q000737:chemistry; D009844:Oligosaccharides / Q000737:chemistry; D051381:Rats; D011994:Recombinant Proteins / Q000737:chemistry; D013213:Starch / Q000737:chemistry; D013394:Sucrase-Isomaltase Complex / Q000737:chemistry*; D000520:alpha-Glucosidases / Q000737:chemistry*
chemical_list: D004187:Disaccharides; D009844:Oligosaccharides; D011994:Recombinant Proteins; D008320:Maltose; D013213:Starch; D013394:Sucrase-Isomaltase Complex; D000520:alpha-Glucosidases; D005947:Glucose
keywords: carbohydrate digestion; disaccharides; glycemic; slowly digestible carbohydrates; α-glucosidases