title: Dietary phenolic compounds selectively inhibit the individual subunits of maltase-glucoamylase and sucrase-isomaltase with the potential of modulating glucose release.
abstract: In this study, it was hypothesized that dietary phenolic compounds selectively inhibit the individual C- and N-terminal (Ct, Nt) subunits of the two small intestinal α-glucosidases, maltase-glucoamylase (MGAM) and sucrase-isomaltase (SI), for a modulated glycemic carbohydrate digestion. The inhibition by chlorogenic acid, caffeic acid, gallic acid, (+)-catechin, and (-)-epigallocatechin gallate (EGCG) on individual recombinant human Nt-MGAM and Nt-SI and on mouse Ct-MGAM and Ct-SI was assayed using maltose as the substrate. Inhibition constants, inhibition mechanisms, and IC50 values for each combination of phenolic compound and enzymatic subunit were determined. EGCG and chlorogenic acid were found to be more potent inhibitors for selectively inhibiting the two subunits with highest activity, Ct-MGAM and Ct-SI. All compounds displayed noncompetitive type inhibition. Inhibition of fast-digesting Ct-MGAM and Ct-SI by EGCG and chlorogenic acid could lead to a slow, but complete, digestion of starch for improved glycemic response of starchy foods with potential health benefit.
authors: †Whistler Center for Carbohydrate Research and Department of Food Science, Purdue University, West Lafayette, Indiana 47907, United States.
authors: Meric
authors: M
authors: Simsek
authors: §Department of Chemistry, Universidad Autonoma de San Luis Potosi, San Luis Potosi, Mexico.|#USDA-ARS, Children's Nutrition Research Center, Department of Pediatrics, Baylor College of Medicine, Houston, Texas 77030, United States.
authors: Roberto
authors: R
authors: Quezada-Calvillo
authors: †Whistler Center for Carbohydrate Research and Department of Food Science, Purdue University, West Lafayette, Indiana 47907, United States.
authors: Mario G
authors: MG
authors: Ferruzzi
authors: #USDA-ARS, Children's Nutrition Research Center, Department of Pediatrics, Baylor College of Medicine, Houston, Texas 77030, United States.
authors: Buford L
authors: BL
authors: Nichols
authors: †Whistler Center for Carbohydrate Research and Department of Food Science, Purdue University, West Lafayette, Indiana 47907, United States.
authors: Bruce R
authors: BR
authors: Hamaker
mesh_terms: D000818:Animals; D004063:Digestion; D004791:Enzyme Inhibitors / Q000737:chemistry* / Q000378:metabolism; D005087:Glucan 1,4-alpha-Glucosidase / Q000737:chemistry* / Q000378:metabolism; D005947:Glucose / Q000737:chemistry*; D006801:Humans; D007700:Kinetics; D051379:Mice; D009834:Oligo-1,6-Glucosidase / Q000737:chemistry* / Q000378:metabolism; D019800:Phenol / Q000737:chemistry* / Q000378:metabolism; D013393:Sucrase / Q000737:chemistry* / Q000378:metabolism; D000520:alpha-Glucosidases / Q000737:chemistry* / Q000378:metabolism
chemical_list: D004791:Enzyme Inhibitors; D019800:Phenol; D009834:Oligo-1,6-Glucosidase; D000520:alpha-Glucosidases; D005087:Glucan 1,4-alpha-Glucosidase; D013393:Sucrase; D005947:Glucose
keywords: inhibition; maltase-glucoamylase; phenolics; sucrase-isomaltase; α-glucosidases