Unexpected High Digestion Rate of Cooked Starch by the Ct-Maltase-Glucoamylase Small Intestine Mucosal α-Glucosidase Subunit

نویسندگان

  • Amy Hui-Mei Lin
  • Buford L. Nichols
  • Roberto Quezada-Calvillo
  • Stephen E. Avery
  • Lyann Sim
  • David R. Rose
  • Hassan Y. Naim
  • Bruce R. Hamaker
چکیده

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%, while other subunits showed 20 to 30% digestion. These findings suggest that Ct-MGAM assists α-amylase in digesting starch molecules and potentially may compensate for developmental or pathological amylase deficiencies.

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منابع مشابه

Unexpected High Digestion Rate of Cooked Starch by the Ct-Maltase-Glucoamylase Small Intestine Mucosal α-Glucosidase Subunit

For starch digestion to glucose, two luminal a-amylases and four gut mucosal a-glucosidase subunits are employed. The aim of this research was to investigate, for the first time, direct digestion capability of individual mucosal a-glucosidases on cooked (gelatinized) starch. Gelatinized normal maize starch was digested with Nand C-terminal subunits of recombinant mammalian maltase-glucoamylase ...

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Direct starch digestion by sucrase-isomaltase and maltase-glucoamylase.

1. Jane J, Chen YY, Lee LF, et al. Effects of amylopectin branch chain length and amylose content on the gelatinization and pasting properties of starch. Cereal Chem 1999;76:629–37. 2. Quezada-Calvillo R, Robayo-Torres CC, Opekum AR, et al. Contribution of mucosal maltase-glucoamylase activities to mouse small intestinal starch alpha-glucogenesis. J Nutr 2007;137:1725–33. 3. Nichols BL, Quezada...

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Contribution of mucosal maltase-glucoamylase activities to mouse small intestinal starch alpha-glucogenesis.

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Clinical aspects and treatment of congenital sucrase-isomaltase deficiency.

30. Chantret I, Lacasa M, Chevalier G, et al. Sequence of the complete cDNA and the 50 structure of the human sucrase-isomaltase gene. Possible homology with a yeast glucoamylase. Biochem J 1992; 285:915–23. 31. Nichols BL, Eldering J, Avery S, et al. Human small intestinal maltaseglucoamylase cDNA cloning. Homology to sucrase-isomaltase. J Biol Chem 1998;273:3076–81. 32. Nichols BL, Avery S, S...

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عنوان ژورنال:

دوره 7  شماره 

صفحات  -

تاریخ انتشار 2012