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Action of human small intestinal brush border carbohydrate digesting enzymes is thought to involve only final hydrolysis reactions of oligosaccharides to monosaccharides. In vitro starch digestibility assays use fungal amyloglucosidase to provide this function. In this study, recombinant N-terminal subunit enzyme of human small intestinal maltase-glucoamylase (rhMGAM-N) was used to explore digestion of native starches from different botanical sources. The susceptibilities to enzyme hydrolysis varied among the starches. The rate and extent of hydrolysis of amylomaize-5 and amylomaize-7 into glucose were greater than for other starches. Such was not observed with fungal amyloglucosidase or pancreatic α-amylase. The degradation of native starch granules showed a surface furrowed pattern in random, radial, or tree-like arrangements that differed substantially from the erosion patterns of amyloglucosidase or α-amylase. The evidence of raw starch granule degradation with rhMGAM-N indicates that pancreatic α-amylase hydrolysis is not a requirement for native starch digestion in the human small intestine. © 2007 Federation of European Biochemical Societies.
Enzyme; Granule; Human; Maltase-glucoamylase; Small intestine; Starch alpha glucosidase; amylase; amylomaize 5; amylomaize 7; fungal enzyme; glucan 1,4 alpha glucosidase; glucose; recombinant enzyme; starch; unclassified drug; animal cell; article; controlled study; digestion; enzymatic degradation; enzyme subunit; hydrolysis; nonhuman; priority journal; scanning electron microscopy; alpha-Amylase; alpha-Glucosidases; Digestion; Glucan 1,4-alpha-Glucosidase; Humans; Hydrolysis; Intestine, Small; Kinetics; Manihot; Pancreas; Recombinant Proteins; Rhizopus; Starch; Zea mays
Evidence of native starch degradation with human small intestinal maltase-glucoamylase (recombinant)
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RDF description of Evidence of native starch degradation with human small intestinal maltase-glucoamylase (recombinant) - http://orbis.uaslp.mx/vivo/individual/scopus1822
Canadian Institutes of Health Research, CIHR: MOP-13338
Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung, SNF: 3100A0-100772
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