Unexpected high digestion rate of cooked starch by the Ct-maltase-glucoamylase small intestine mucosal α-glucosidase subunit
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For starch digestion to glucose, two luminal α-amylases and four gut mucosal α-glucosidase subunits are employed. The aim of this research was to investigate, for the first time, direct digestion capability of individual mucosal α-glucosidases on cooked (gelatinized) starch. Gelatinized normal maize starch was digested with N- and C-terminal subunits of recombinant mammalian maltase-glucoamylase (MGAM) and sucrase-isomaltase (SI) of varying amounts and digestion periods. Without the aid of α-amylase, Ct-MGAM demonstrated an unexpected rapid and high digestion degree near 80%25, while other subunits showed 20 to 30%25 digestion. These findings suggest that Ct-MGAM assists α-amylase in digesting starch molecules and potentially may compensate for developmental or pathological amylase deficiencies. © 2012 Lin et al.
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alpha glucosidase; cooked starch; recombinant enzyme; starch; sucrase isomaltase; unclassified drug; alpha glucosidase; amylase; gelatin; recombinant protein; amino terminal sequence; article; carbohydrate analysis; carboxy terminal sequence; concentration response; controlled study; cooking; digestion; enzyme activity; incubation time; maize; mammal; small intestine mucosa; animal; digestion; enzymology; genetics; heat; human; intestine mucosa; metabolism; mouse; protein subunit; small intestine; Mammalia; Zea mays; alpha-Amylases; alpha-Glucosidases; Animals; Cooking; Digestion; Gelatin; Hot Temperature; Humans; Intestinal Mucosa; Intestine, Small; Mice; Protein Subunits; Recombinant Proteins; Starch
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