• Nutritional Sciences
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• v.8 no.4
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• pp.226-230
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• 2005

To keep blood glucose levels as close to normal as possible is the major goal of diabetes mellitus treatment $\alpha$-Glucosidase is the enzyme that digests die1my carbohydrate and inhibition of this enzyme may suppress postprandial hyperglycemia. The methanol extract of Polygonum multiflorum Thunberg was tested for inhibitoty activity against $\alpha$-glucosidase in vitro and in vivo. Polygonum multiflorum Thunberg extract inhibited yeast $\alpha$-glucosidase activity in a concentration-dependent manner. Polygonum multiflorum Thunberg showed an $IC_{50}$ value of 0.48 mg/mL. The ability of Polygonum multiflorum Thunberg extract to lower postprandial glucose was studied in streptozotocin-induced diabetic rats. A starch solution (1 g/kg) with and without the methanol extract of Polygonum multiflorum Thunberg extract (500 mg/kg) was administered to diabetic rats by gastric intubation after an overnight fast A single oral dose of Polygonum multiflorum Thunberg extract significantly inhibited increases in blood glucose levels at 60 and 90 min (p<0.05) and significantly decreased incremental response areas under the glycemic response curve (p<0.05). These results suggest that Polygonum multiflorum Thunberg may have an antihyperglycemic effect by inhibiting $\alpha$-glucosidase activity in the animal model of diabetes mellitus.

• Korean Journal of Food Science and Technology
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• v.32 no.3
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• pp.618-628
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• 2000

The indigestible dextrin I was prepared by hydrolyzing pyrodextrin with thermostable ${\alpha}-amylase$. The mean values of indigestible fraction and dieatry fiber of indigestible dextrin I prepared from yellow dextrin were 50.0% and 25.0%, respectively. Also the indigestible dextrin II was prepared by removing low molecular weight saccharides containing glucose with ethanol from enzyme hydrolysate of pyrodextrins. Over 80% of glucose and maltose in initial enzyme hydrolysate were removed, therefore the indigestible fraction and dietary fiber of the indigestible dextrins increased. The indigestible dextrin from ethanol precipitate of enzyme hydrolysate of yellow dextrin by ${\alpha}-amylase$ and amyloglucosidase showed a higher contents of indigestible fraction and dietary fiber than ethanol precipitates by any other enzyme combination, and its mean values were 83.6% and 62.8%, respectively. Consequently, it was found that the indigestible dextrins which are resistant to starch-hydrolysing enzyme can be easily prepared from pyrodextrin, and presumed that they can perform physiological functions as soluble dietary fiber.

• Food Science and Biotechnology
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• v.18 no.3
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• pp.808-812
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• 2009

The ${\alpha}-glucosidase$ inhibitory and antioxidant effects of water chestnut (Trapa japonica Flerov.) were assessed to explore its possible use as an anti-diabetic agent. Methanol extracts of the fruit shell and meat of water chestnut were assayed for inhibitory activity against yeast ${\alpha}-glucosidase$ and 1,1-diphenyl-2-picrylhydrazyl (DPPH) radical scavenging activity. Effect of fruit shell extract on postprandial glucose response was assessed. Compared with fruit meat, shell extract showed stronger inhibition against ${\alpha}-glucosidase$ with an $IC_{50}$ of 273 ${\mu}g/mL$. Oral administration of fruit shell extract (500 mg/kg) significantly lowered the postprandial area under the glucose response curve to starch (1 g/kg) in streptozotocin (STZ)-induced diabetic rats (p<0.01). Compared with fruit meat, shell extract showed stronger scavenging activity against DPPH, with an $IC_{50}$ of 27.1 ${\mu}g/mL$. The results indicate that the fruit shell of water chestnut was effective in controlling postprandial hyperglycemia and exerted an antioxidant effect. Therefore, water chestnut may be useful in treating diabetes.

• Journal of Microbiology and Biotechnology
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• v.23 no.1
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• pp.56-63
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• 2013

We have characterized the putative ${\alpha}$-glucosidase gene (st2525) selected by total genome analysis from the acidothermophilic crenarchaeon Sulfolobus tokodaii strain 7. The ORF was cloned and expressed as a fusion protein in Escherichia coli, and recombinant ST2525 was purified by Ni-NTA affinity chromatography. Maximum activity was observed at $95^{\circ}C$ and pH 4.0, and the enzyme exhibited stability with half-lives of 40.1 min and 7.75 min at extremely high temperatures of $100^{\circ}C$ and $105^{\circ}C$, respectively. The enzyme retained at least 85% of its maximal activity in the pH range of 4.0-11.0. ST2525 exclusively hydrolyzed ${\alpha}$-1,4-glycosidic linkages of oligosaccharides in an exo-type manner, with highest catalytic efficiency toward maltotriose. The enzyme also displayed transglycosylation activity, converting maltose to isomaltose, panose, maltotriose, isomaltotriose, etc. From these results, ST2525 could be potentially useful for starch hydrolysis as well as novel synthesis of oligosaccharides in industry.

• Journal of Microbiology and Biotechnology
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• v.29 no.5
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• pp.765-775
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• 2019

A new ${\alpha}$-amylase-encoding gene (amySL3) of glycoside hydrolase (GH) family 13 was identified in soda lake isolate Alkalibacterium sp. SL3. The deduced AmySL3 shares high identities (82-98%) with putative ${\alpha}$-amylases from the genus Alkalibacterium, but has low identities (<53%) with functionally characterized counterparts. amySL3 was successfully expressed in Escherichia coli, and the recombinant enzyme (rAmySL3) was purified to electrophoretic homogeneity. The optimal temperature and pH of the activity of the purified rAmySL3 were determined to be $45^{\circ}C$ and pH 7.5, respectively. rAmySL3 was found to be extremely halophilic, showing maximal enzyme activity at a nearly saturated concentration of NaCl. Its thermostability was greatly enhanced in the presence of 4 M NaCl, and it was highly stable in 5 M NaCl. Moreover, the enzyme did not require calcium ions for activity, and was strongly resistant to a range of surfactants and hydrophobic organic solvents. The major hydrolysis products of rAmySL3 from soluble starch were maltobiose and maltotriose. The high ratio of acidic amino acids and highly negative electrostatic potential surface might account for the halophilic nature of AmySL3. The extremely halophilic, calcium-independent, and surfactant-resistant properties make AmySL3 a promising candidate enzyme for both basic research and industrial applications.

• Nutrition Research and Practice
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• v.4 no.6
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• pp.486-491
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• 2010

Tight control of blood glucose is the most important strategy for the treatment of diabetes mellitus. Here, we investigated the beneficial effects of Welsh onion on fasting and postprandial hyperglycemia. Inhibitory activities of hot water extracts from the green stalk and white bulb, which are the edible portions of the Welsh onion, and the fibrous root extract against yeast ${\alpha}$-glucosidase were measured in vitro. To study the effects of Welsh onion on postprandial hyperglycemia, a starch solution (1 g/kg) with and without Welsh onion fibrous root extract (500 mg/kg) or acarbose (50 mg/kg) was administered to streptozotocin-induced diabetic rats after an overnight fast. Postprandial plasma glucose levels were measured and incremental areas under the response curve were calculated. To study the hypoglycemic effects of chronic feeding of Welsh onion, five-week-old db/db mice were fed an AIN-93G diet or a diet containing either Welsh onion fibrous root extract at 0.5% or acarbose at 0.05% for 7 weeks after 1 week of adaptation. Fasting plasma glucose and blood glycated hemoglobin were measured. Compared to the extract from the edible portions of Welsh onion, the fibrous root extract showed stronger inhibition against yeast ${\alpha}$-glucosidase, with an $IC_{50}$ of 239 ${\mu}g/mL$. Oral administration of Welsh onion fibrous root extract (500 mg/kg) and acarbose (50 mg/kg) significantly decreased incremental plasma glucose levels 30-120 min after oral ingestion of starch as well as the area under the postprandial glucose response curve, compared to the control group (P < 0.01). The plasma glucose and blood glycated hemoglobin levels of the Welsh onion group were significantly lower than those of the control group (P < 0.01), and were not significantly different from those fed acarbose. Thus, we conclude that the fibrous root of Welsh onion is effective in controlling hyperglycemia in animal models of diabetes mellitus.

• Korean Journal of Food Science and Technology
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• v.48 no.4
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• pp.341-346
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• 2016

The AMY2B gene, encoding human pancreatic ${\alpha}$-amylase isozyme (HPA II), was expressed in Pichia pastoris, and the effects of chloride ions on HPA II activity toward starch substrates were investigated. As seen with chloride ion-dependent ${\alpha}$-amylases-including HPA I, the isozyme of HPA II-chloride ions increased enzyme activity and shifted the optimal pH to an alkaline pH. The activity enhancement by chloride was more significant at pH 8 than that at pH 6, suggesting that the protonation state of the general acid/base catalyst of HPA II was important for the hydrolysis of starches at an alkaline pH because of the increase in its $pK_a$ by chloride ions. The turnover values for cereal starches as the substrates markedly increased in the presence of chloride by up to 7.2-fold, whereas that for soluble starch increased by only 1.7-fold. Chloride inhibited substrate hydrolysis at high substrate concentrations, with $K_i$ values ranging from 6 to 15 mg/mL.

• KSBB Journal
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• v.10 no.3
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• pp.304-316
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• 1995

For fuel alcohol production, enzymatic liquefaction and saccharification of tapioca starch by ${\alpha}$-amylase and glucoamylase were studied. The thermophilic ${\alpha}$-amylase Termamyl produced from Bacillus licheniformis gave a better liquefaction than the relalively low temperature enzyme BAN from B. subtilis. Oplimal temperature and pH with Termamyl were $90∼95^{\circ}C$ and 5.8, respectively. Minimal amount of Termamyl 240uc for a satisfactory liquefaction for a two-hour reaction was about 0.0125% (v/w) with respect to the mass of tapioca used. For saccharification experiments two enzymes, Novo AMG and Do-I1 enzymes were compared. The enzymatic activity of each enzyme was a little different depending on the substrate used and the latter was found to have a significant amount of ${\alpha}$-amylase activity. With Novo AMG optimal temperature was about $58^{\circ}C$ The pH optimum was 4.3 with maltose, however, with tapioca, no difference was observed between pH 4.3 and 5.7 which is a natural, unadjusted pH of liquefied tapioca. For 85% of completion of saccharification, it was necessary to use 0.0625% (v/w) of Novo AMG 400L for tapioca and to run the reaction for more than 10 hr, Packed volume of solid particles in tapioca slurry remained at around 30% during liquefaction and saccharification. This indicates that the removal of the solid particle before fermentation is not economically feasible at all, even though the solid particles make it very difficult to operate the bioreactor in a continuous mode with cell-recycle.

• Korean Journal of Food Science and Technology
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• v.20 no.4
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• pp.504-510
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• 1988

The physicochemical properties of rice flours which were obtained by dry milling(blade, hammer, test and micro mill) and wet & dry milling (roller & micro mill) were investigated. The resulting flour particle sizes were reduced in the order that of blade, hammer, test, micro and roller & micro mill. Scanning electron microscopic examination showed that the starch granules were freed from the imbedding matrix as the particles became finer. The test-milled flour had the hightest levels of starch damage, maltose value and hot-water soluble amylose content, and the blade-milled flour showed the lowest levels. Amylograph viscosity and gelatinization temperature of the flours decreased as the particles became finer, and the addition of $Hg^{+2}$ increased the peak viscosity of the dry-milled flour pastes, whereas the wet & dry-milled flour did not show any changes. The blue values and ${\lambda}$max values of the iodine complex of the cold-water extractable ${\alpha}-D-glucan$ from flours were in the range of 0.023-0.029 and 518-522nm, respectively, indicating these materials were shown to be mainly composed of amylopectin-like polymer.

• Preventive Nutrition and Food Science
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• v.7 no.3
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• pp.310-316
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• 2002

Extracellular cyclodextrin glucanotransferase (CGTase) from Paenibacillus sp. JK-12 was purified through sev-eral purification steps consisting of ammonium sulfate precipitation and chromatographies on DEAE-sephadex A-50 and Mono QIM HR5/5. The purified CGTase exhibited a single band on SDS-PAGE and was estimated to be approximately 82 kDa. The isoelectric point of the enzyme was 7.2 as determined by isoelectric focusing. The CGTase from Paenibacillus sp. JK-12 had a transglucosylation activity at the C-2 position of L-ascorbic acid. The optimum pH and temperature for the CGTase activity were 8.0 and 5$0^{\circ}C$, respectively. The enzyme activity was stable from pH 6.0 to 9.() and at temperatures up to 55$^{\circ}C$ at pB 8.0, having 80% residual activity. The activity of the CGTase was strongly resistant to metals such as A $g^{+}$ and $Ba^{2+}$ but slightly inhibited by H $g^{+}$, N $i^{2+}$ and $Mg^{2+}$. The enzymeproduced $\alpha$ -cyclodextrin ($\alpha$-CD) and $\beta$-CD as the main products from starch, but not ${\gamma}$-CD.X>-CD.