2016
DOI: 10.1021/acs.jafc.6b01816
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Contribution of the Individual Small Intestinal α-Glucosidases to Digestion of Unusual α-Linked Glycemic Disaccharides

Abstract: The mammalian mucosal α-glucosidase complexes, maltase-glucoamylase (MGAM) and sucrase-isomaltase (SI), have two catalytic subunits (N- and C-termini). Concurrent with the desire to modulate glycemic response, there has been a focus on di-/oligosaccharides with unusual α-linkages that are digested to glucose slowly by these enzymes. Here, we look at disaccharides with various possible α-linkages and their hydrolysis. Hydrolytic properties of the maltose and sucrose isomers were determined using rat intestinal … Show more

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Cited by 102 publications
(91 citation statements)
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“…20,21,46 These enzymatic structures could also have more versatility in terms of hydrolytic activity, as was showed elsewhere. 16,47 To the best of our knowledge, these data are the first evidence about digestibility of α-GOS with small intestine enzymes.…”
Section: Digestion Of Prebiotic Carbohydrates Using Rsiementioning
confidence: 63%
“…20,21,46 These enzymatic structures could also have more versatility in terms of hydrolytic activity, as was showed elsewhere. 16,47 To the best of our knowledge, these data are the first evidence about digestibility of α-GOS with small intestine enzymes.…”
Section: Digestion Of Prebiotic Carbohydrates Using Rsiementioning
confidence: 63%
“…Considering this proximity, and that α-glucosidases are the two most abundant proteins in the orange colored bands (see below), we suspect that the bands indicated by the arrows on the Coomassie blue stained gel correspond to SI and MGAM, but additional tests (e.g., Western blots) would be necessary to confirm this. Because electrophoretic mobility of native proteins results from size and charge as well as the overall bulk or cross-sectional area of the protein, Mr markers do not allow the exact determination of the Mr of test proteins [17]. Additionally, the differences in migration over the polyacrylamide gel between the weight marker and the band that contains the α-glucosidases might also be due to the level of glycosylation of these two proteins [4,18].…”
Section: Resultsmentioning
confidence: 99%
“…The common glycosidic bonds that are digestible by humans include (a1!4) and (a1!6) glucose-glucose that make up (iso)maltose, (iso)maltooligosaccharides, and starch; sucrose, (a1!2) glucose-fructose; and lactose, (b1!4) galactose-glucose. Uncommon linkages that can be hydrolyzed by the a-glucosidases include (a1!1), (a1!2), and (a1!3) glucose-glucose; and (a1!3), (a1!4), (a1!5), and (a1!6) glucose-fructose (Lee et al 2016). When multiple monosaccharides are linked together, they form polysaccharides, which are used for energy storage and structure.…”
Section: Glycemic Carbohydrates and Their Structurementioning
confidence: 99%
“…The ability of the mammalian a-glucosidases to hydrolyze different a-linked glucose-glucose disaccharides has been studied using recombinantly expressed and purified enzymes. Glucoamylase was shown to act (enzyme efficiency of glucose generation) on maltose (a1!4) (K cat /K m 51.0 mM À1 s À1 ), kojibiose (a1!2) (K cat /K m 0.9 mM À1 s À1 ), and nigerose (a1!3) (K cat /K m 2.7 mM À1 s À1 ); with higher maltase activity than the maltase subunit itself (K cat /K m 51.0 vs. 12.7 mM À1 s À1 ) (Lee et al 2016). Glucoamylase is reported to be inhibited by maltotriose and maltotetraose at high concentrations (Quezada-Calvillo et al 2008).…”
Section: The Enzymes Responsible For Mammalian A-glucan Digestionmentioning
confidence: 99%