Slow glucose release property of enzyme-synthesized highly branched maltodextrins differs among starch sources

Kittisuban, Phatcharee; Lee, Byung‐Hoo; Suphantharika, Manop; Hamaker, Bruce R.

doi:10.1016/j.carbpol.2014.02.033

Cited by 77 publications

(58 citation statements)

References 33 publications

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“…1D). These results are in agreement with previous investigations (Kittisuban, Lee, Suphantharika and Hamaker, 2014;Roussel et al, 2013) using R. obamensis BE with selected types of starches as substrate. Interestingly, the chains in the BEAMBE modified starches clearly showed a distributional trend characterized by an increase in short chains of DP 3-12 with higher AO substrate content (Fig.…”

Section: Chain-length Distributionsupporting

confidence: 93%

“…This result demonstrates an effect of AM on arrangement the α-glucan structure due to it disproportionation activity of the α-glucan linear chains or clusters. In addition, a previous study demonstrated that α-glucan hydrolysis rate by MGAM-SI is low on densely branched α-limit dextrin (Kittisuban et al, 2014;. Particular chemical structures including tightly branched clustered in the α-limit dextrin can affect the MGAM-SI catalysis (Lin et al, 2010).…”

Section: Glucose Released After Rat Intestinal α-Glucosidases Hydrolysismentioning

confidence: 99%

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Structure of branching enzyme- and amylomaltase modified starch produced from well-defined amylose to amylopectin substrates

Sorndech¹,

Sagnelli

Meier

et al. 2016

Carbohydrate Polymers

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Highlights •Enzyme modification of starch systems with well-defined amylose:amylopectin ratios provides detailed insight into the effects of substrate branching on enzymatic chain transfer • High amylose substrates produce high branching rates, high M w, short chains and low amylolytic digestion when treated with branching enzyme alone or in combination with amylomaltase.• Not only branching density but also molar mass of the glucan product restricts dietary degradation by steric hindrance towards human pancreatic α-amylase and α-glucosidases. AbstractThermostable branching enzyme (BE, EC 2.4.1.18) from Rhodothermus obamensis in combination with amylomaltase (AM, EC 2.4.1.25) from Thermus thermophilus was used to modify starch structure exploring potentials to extensively increase the number of branch points in starch. Amylose is an important constituent in starch and the effect of amylose on enzyme catalysis was investigated using amylose-only barley starch (AO) and waxy maize starch (WX) in well-defined ratios. All products were analysed for amylopectin chain length distribution, α-1,6 glucosidic linkages content, molar mass distribution and digestibility by using rat intestinal α-glucosidases. For each enzyme treatment series, increased AO content resulted in a higher rate of α-1,6 glucosidic linkage formation but as an effect of the very low initial branching of the AO, the final content of α-1,6 glucosidic linkages was slightly lower as compared to the high amylopectin substrates. However, an increase specifically in short chains was produced at high AO levels. The molar mass distribution for the enzyme treated samples was lower as compared with substrate WX and AO, indicating the presence of hydrolytic activity as well as cyclisation of the substrate. For all samples, increased amylose substrate showed decreased α-and β-amylolysis. Surprisingly, hydrolysis with rat intestinal α-glucosidases was higher with increasing α-1,6 glucosidic linkage content and decreasing M w indicating that steric hindrance towards the α-glucosidases was directed by the molar mass rather that the branching density of the glucan per se. Our data demonstrate that a higher amylose content in the substrate starch efficiently produces α-1,6 glucosidic linkages and that the present of amylose generates a higher M w and more resistant product than amylopectin. The combination of BEAMBE provided somewhat more resistant α-glucan products as compared to BE alone.

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Section: Chain-length Distributionsupporting

confidence: 93%

Section: Glucose Released After Rat Intestinal α-Glucosidases Hydrolysismentioning

confidence: 99%

Structure of branching enzyme- and amylomaltase modified starch produced from well-defined amylose to amylopectin substrates

Sorndech¹,

Sagnelli

Meier

et al. 2016

Carbohydrate Polymers

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“…In the human digestive system, the ␣1¡6 linkages in starch are hydrolyzed at a lower rate than ␣1¡4 linkages (12, 13). Branching enzymes, alone or in combination with ␤-amylase, are used to increase the percentage of ␣1¡4,6 branches in starches (12)(13)(14).The 4,6-␣-glucanotransferase (4,6-␣-GTase) enzymes, such as GTFB, GTFW, and GTFML4, of Lactobacillus reuteri strains constitute a subfamily of glycoside hydrolase family 70 (GH70); GH70 mainly consists of glucansucrases (GSes) (http://www.cazy.org). Unlike GSes, 4,6-␣-GTases are not sucrose-acting enzymes but rather starch-converting enzymes, capable of converting (1¡4)-␣-D-gluco-oligosaccharides into dietary fiber isomalto/maltopolysaccharides (IMMPs).…”

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confidence: 99%

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confidence: 99%

“…Slowly digestible starch materials prepared by physical processing suffer losses upon boiling; therefore, structural modifications through enzymatic treatment of starch are more desirable. In the human digestive system, the ␣1¡6 linkages in starch are hydrolyzed at a lower rate than ␣1¡4 linkages (12,13). Branching enzymes, alone or in combination with ␤-amylase, are used to increase the percentage of ␣1¡4,6 branches in starches (12)(13)(14).…”

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Biochemical Characterization of the Lactobacillus reuteri Glycoside Hydrolase Family 70 GTFB Type of 4,6-α-Glucanotransferase Enzymes That Synthesize Soluble Dietary Starch Fibers

Bai

Kaaij

Leemhuis

et al. 2015

Appl Environ Microbiol

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c 4,6-␣-Glucanotransferase (4,6-␣-GTase) enzymes, such as GTFB and GTFW of Lactobacillus reuteri strains, constitute a new reaction specificity in glycoside hydrolase family 70 (GH70) and are novel enzymes that convert starch or starch hydrolysates into isomalto/maltopolysaccharides (IMMPs). These IMMPs still have linear chains with some ␣1¡4 linkages but mostly (relatively long) linear chains with ␣1¡6 linkages and are soluble dietary starch fibers. 4,6-␣-GTase enzymes and their products have significant potential for industrial applications. Here we report that an N-terminal truncation (amino acids 1 to 733) strongly enhances the soluble expression level of fully active GTFB-⌬N (approximately 75-fold compared to full-length wild type GTFB) in Escherichia coli. In addition, quantitative assays based on amylose V as the substrate are described; these assays allow accurate determination of both hydrolysis (minor) activity (glucose release, reducing power) and total activity (iodine staining) and calculation of the transferase (major) activity of these 4,6-␣-GTase enzymes. The data show that GTFB-⌬N is clearly less hydrolytic than GTFW, which is also supported by nuclear magnetic resonance (NMR) analysis of their final products. From these assays, the biochemical properties of GTFB-⌬N were characterized in detail, including determination of kinetic parameters and acceptor substrate specificity. The GTFB enzyme displayed high conversion yields at relatively high substrate concentrations, a promising feature for industrial application. Starch is the second-most-abundant carbohydrate on earth and a major dietary carbohydrate for humans; as a storage carbohydrate it is present in seeds, roots, and tubers of plants (1). It consists of ␣-glucan polymers with ␣1¡4 linkages and a low percentage of ␣1¡6 linkages, in the form of amylose and branched amylopectin (2). Starches are applied in various industrial products such as food, paper, and textiles, often after processing by physical, chemical, or enzymatic treatment (3-6).Dietary fibers and low-glycemic-index (low-GI) food are considered healthy food contributing to our long-term well-being (7,8). Of all the nutritional types of starch, slowly digestible starch with low GI has drawn the strongest interest. Annealing/heatmoisture treatment, recrystallization, and enzymatic treatment are recognized approaches to obtain slowly digestible starch (9-11). Slowly digestible starch materials prepared by physical processing suffer losses upon boiling; therefore, structural modifications through enzymatic treatment of starch are more desirable. In the human digestive system, the ␣1¡6 linkages in starch are hydrolyzed at a lower rate than ␣1¡4 linkages (12, 13). Branching enzymes, alone or in combination with ␤-amylase, are used to increase the percentage of ␣1¡4,6 branches in starches (12)(13)(14).The 4,6-␣-glucanotransferase (4,6-␣-GTase) enzymes, such as GTFB, GTFW, and GTFML4, of Lactobacillus reuteri strains constitute a subfamily of glycoside hydrolase family 70 (GH70); GH70 ...

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Novel Ingredients from Cereals

Agyei

Jeevanandam

Dzuvor

et al. 2020

Innovative Processing Technologies for Healthy Grains

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Slow glucose release property of enzyme-synthesized highly branched maltodextrins differs among starch sources

Cited by 77 publications

References 33 publications

Structure of branching enzyme- and amylomaltase modified starch produced from well-defined amylose to amylopectin substrates

Structure of branching enzyme- and amylomaltase modified starch produced from well-defined amylose to amylopectin substrates

Biochemical Characterization of the Lactobacillus reuteri Glycoside Hydrolase Family 70 GTFB Type of 4,6-α-Glucanotransferase Enzymes That Synthesize Soluble Dietary Starch Fibers

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