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Mucosal C-terminal maltase-glucoamylase hydrolyzes large size starch digestion products that may contribute to rapid postprandial glucose generation
type: Article
doi: 10.1002/mnfr.201300599
crisid: 3823
chemicalscas: alpha glucosidase, 9001-42-7; amylase, 9000-90-2, 9000-92-4, 9001-19-8; glucose, 50-99-7, 84778-64-3; maltodextrin, 9050-36-6; maltose, 16984-36-4, 69-79-4; starch, 9005-25-8, 9005-84-9; alpha-Amylases; alpha-Glucosidases; Blood Glucose; Glucose; maltodextrin; maltooligosaccharides; Maltose; maltotetraose; Oligosaccharides; Polysaccharides; Recombinant Proteins; Starch
type: Document
related by: authorship_22059
e iscopus: 2-s2.0-84898946600
type: Generically Dependent Continuant
origen: scopus
estado: published
related by: authorship_22057
type: Thing
type: Information Content Entity
abstract: Scope: The four mucosal α-glucosidases, which differ in their digestive roles, generate glucose from glycemic carbohydrates and accordingly can be viewed as a control point for rate of glucose delivery to the body. In this study, individual recombinant enzymes were used to understand how α-glucan oligomers are digested by each enzyme, and how intermediate α-amylolyzed starches are hydrolyzed, to elucidate a strategy for moderating the glycemic spike of rapidly digestible starchy foods. Methods and results: The C-terminal maltase-glucoamylase (ctMGAM, commonly termed glucoamylase) was able to rapidly hydrolyze longer maltooligosaccharides, such as maltotetraose and maltopentaose, to glucose. Moreover, it was found to convert larger size maltodextrins, as would be produced early in α-amylase digestion of starch, efficiently to glucose. It is postulated that ctMGAM has the additional capacity to hydrolyze large α-amylase products that are produced immediately on starch digestion in the duodenum and contribute to the rapid generation of glucose from starch-based meals. Conclusion: The findings suggest that partial inhibition of ctMGAM, such as by natural inhibitors found in foods, might be used to moderate the early stage of high glycemic response, as well as to extend digestion distally; thereby having relevance in regulating glucose delivery to the body. © 2014 WILEY-VCH Verlag GmbH %26 Co. KGaA, Weinheim.
related by: authorship_22056
page start: 1111
related by: authorship_22062
date time value: article date 3823
volume: 58
related by: authorship_22061
type: Continuant
issue: 5
most specific type: Article
related by: authorship_22058
type: Entity
most specific type: Document
pmid: 24442968
related by: authorship_22060
abstract: Scope: The four mucosal α-glucosidases, which differ in their digestive roles, generate glucose from glycemic carbohydrates and accordingly can be viewed as a control point for rate of glucose delivery to the body. In this study, individual recombinant enzymes were used to understand how α-glucan oligomers are digested by each enzyme, and how intermediate α-amylolyzed starches are hydrolyzed, to elucidate a strategy for moderating the glycemic spike of rapidly digestible starchy foods. Methods and results: The C-terminal maltase-glucoamylase (ctMGAM, commonly termed glucoamylase) was able to rapidly hydrolyze longer maltooligosaccharides, such as maltotetraose and maltopentaose, to glucose. Moreover, it was found to convert larger size maltodextrins, as would be produced early in α-amylase digestion of starch, efficiently to glucose. It is postulated that ctMGAM has the additional capacity to hydrolyze large α-amylase products that are produced immediately on starch digestion in the duodenum and contribute to the rapid generation of glucose from starch-based meals. Conclusion: The findings suggest that partial inhibition of ctMGAM, such as by natural inhibitors found in foods, might be used to moderate the early stage of high glycemic response, as well as to extend digestion distally; thereby having relevance in regulating glucose delivery to the body. © 2014 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
page end: 1121
freetext keyword: CtMGAM; Glucogenesis; Glycemic spike; Mucosal α-glucosidases; Starch digestion alpha glucosidase; amylase; glucose; glucose blood level; maltodextrin; maltooligosaccharides; maltose; maltotetraose; oligosaccharide; polysaccharide; recombinant protein; starch; analogs and derivatives; chemistry; digestion; duodenum; glucose blood level; human; hydrolysis; metabolism; mucosa; postprandial state; alpha-Amylases; alpha-Glucosidases; Blood Glucose; Digestion; Duodenum; Glucose; Humans; Hydrolysis; Maltose; Mucous Membrane; Oligosaccharides; Polysaccharides; Postprandial Period; Recombinant Proteins; Starch
has publication venue: Molecular Nutrition and Food Research

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date: 2026-08-24T04:54:31
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label: RDF description of Mucosal C-terminal maltase-glucoamylase hydrolyzes large size starch digestion products that may contribute to rapid postprandial glucose generation - http://orbis.uaslp.mx/vivo/individual/scopus3822

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