• Journal of Microbiology and Biotechnology
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• v.10 no.2
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• pp.244-250
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• 2000

An ${\alpha}-glucosidase$ gene (aglA) from thermophilic Bacillus sp. DG0303 was cloned, sequenced, and expressed in Escherichia coli. The aglA was localized to the 2.1-kb PvuI-XmnI region within the 5.9-kb DNA insert of the gybrid plasmid pAG1. The gene consisted of an open reading frame of 1,686 bp with an unusual GTG initiation codon and TGA termination codon. The amino acid sequence deduced from the nucleotide sequence predicted a protein of 562 amino acid residues with a M, of 66,551 dalton. A comparative amino acid sequence analysis revealed that DG0303 ${\alpha}-glucosidase$ is related to bacillary oligo-1, 6-glucosidases. The Bacillus sp. DG0303 ${\alpha}-glucosidase$ showed a high sequence identity (36-59%) to the B. flavocaldarius, B. cereus, and B. thermoglucosidasius oligo-1, 6-glucosidases. The number of prolines in theses four ${\alpha}-glucosidases. was observed to increase with increasing thermostability of these enzymes. The cloned ${\alpha}-glucosidase was purified from E. coli $DH5{\alpha}$ bearing pAG1 and characterized. The recombinant enzyme was identical with the native enzyme in its optimum pH and in its molecular mass, estimated by sodium dodecy1 sulfate-polyacrylamide gel electrophoresis. The temperature optimum of the cloned ${\alpha}-glucosidase$ was lower than that of the native enzyme.

• Preventive Nutrition and Food Science
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• v.19 no.1
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• pp.5-9
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• 2014

This study was designed to investigate the inhibitory effects of Polyopes lancifolia extract (PLE) on ${\alpha}$-glucosidase activity, ${\alpha}$-amylase activitiy, and postprandial hyperglycemia in streptozotocin (STZ)-induced diabetic mice. The results of this study revealed a marked inhibitory effect of PLE on ${\alpha}$-glucosidase and ${\alpha}$-amylase activities. The $IC_{50}s$ of PLE against ${\alpha}$-glucosidase and ${\alpha}$-amylase were 0.20 mg/mL and 0.35 mg/mL, respectively. PLE was a more effective inhibitor of ${\alpha}$-glucosidase and ${\alpha}$-amylase activities than acarbose, the positive control. The postprandial blood glucose levels of STZ-induced diabetic mice were significantly lower in the PLE treated group than in the control group. Moreover, PLE administration was associated with a decreased area under the curve for the glucose response in diabetic mice. These results indicate that PLE may be a potent inhibitor of ${\alpha}$-glucosidase and ${\alpha}$-amylase activities and may suppress postprandial hyperglycemia.

• Korean Journal of Plant Resources
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• v.26 no.4
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• pp.411-416
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• 2013

This study was conducted not only to analyze ${\alpha}$-glucosidase inhibition activity with fronds and rhizomes of nine Pteridophyte species, but also to select the plant materials suitable for natural ${\alpha}$-glucosidase inhibitor. Harvested rhizomes and fronds were washed, freeze-dried and grinded. After conducting ultrasonification extraction for 30 minutes in ultrasonic water tank with 100% methanol solvent, and vacuum filtration, ${\alpha}$-glucosidase inhibition activity was measured. Acarbose was used as the positive control. After mixing $100{\mu}L$ of 0.7 unit ${\alpha}$-glucosidase enzyme solution into $50{\mu}L$ of extract and reacting them at $37^{\circ}C$ for 10 minutes, $50{\mu}L$ of 1.5 mM ${\rho}$-NPG solution was taken and reacted at $37^{\circ}C$ for 20 minutes. The reaction was stopped with 1 mL of 1 M $Na_2CO_3$ and absorbance was measured in 405 nm. With the regression analysis, the content of solubility solids (the value of $IC_{50}$) which can inhibit 50% of 0.7 unit ${\alpha}$-glucosidase solution's activity was investigated. The frond ($IC_{50}=14.00{\sim}913.33{\mu}g{\cdot}mL^{-1}$) and rhizome extracts ($IC_{50}=12.93{\sim}205.84{\mu}g{\cdot}mL^{-1}$) of nine Pteridophyte species showed higher ${\alpha}$-glucosidase inhibition activity in comparison with acarbose ($IC_{50}=1413.70{\mu}g{\cdot}mL^{-1}$). The extracts of fronds and rhizomes showed higher value than acarbose by 1.55~100.98 and 6.87~109.33 times each. Especially, ${\alpha}$-glucosidase inhibition activities of Pyrrosia lingua in fronds and Osmunda cinnamomea var. fokiensis in rhizomes were the highest. The necessary biomass of fronds and rhizomes for inhibiting 50% of ${\alpha}$-glucosidase activity showed the lowest value, 0.35, 0.27 mg each, in O. cinnamomea var. fokiensis. $IC_{50}$ value of P. lingua was the highest among fronds of nine Pteridophyte species, but content of soluble solids was 2.4 times less than O. cinnamomea var. fokiensis. So frond of O. cinnamomea var. fokiensis is more economic in comparison with P. lingua. As the result of this study, O. cinnamomea var. fokiensis showed high ${\alpha}$-glucosidase inhibition activity even with small biomass. Therefore it was considered to be high-valued economic material as natural ${\alpha}$-glucosidase inhibitor.

• Korean Journal of Medicinal Crop Science
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• v.17 no.5
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• pp.357-362
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• 2009

Compounds of isolated from roots extract of Pueraria thunbergiana were tested their inhibitory effects on $\alpha$-glucosidase and $\alpha$-amylase. Inhibitory activity of methylene chloride (MC) fraction and ethyl acetate (EA) fraction against $\alpha$-glucosidase showed more than 60% at a concentration of $500{\mu}g/m{\ell}$. Among the nine compounds tested on $\alpha$-glucosidase, biochanin A, (-)-tuberosin and calycosin from MC fraction and daidzein from EA fraction were stronger inhibitors than acarbose ($IC_{50}=530{\mu}g/m{\ell}$), and their $IC_{50}$ were 9, 144, 328 and $20{\mu}g/m{\ell}$, respectively. Biochanin A and (-)-tuberosin also inhibited $\alpha$-amylase activity as like as acarbose $IC_{50}=20.5{\mu}g/m{\ell}$), and their $IC_{50}$ were 22 and $348{\mu}g/m{\ell}$, respectively. Although daidzein was already known $\alpha$-glucosidase inhibitory effects, it was newly evaluated that biochanin A and (-)-tuberosin inhibited $\alpha$-glucosidase as well as $\alpha$-amylase, and that calycosin did $\alpha$-glucosidase.

• International Journal of Industrial Entomology and Biomaterials
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• v.15 no.2
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• pp.161-164
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• 2007

While searching for ${\alpha}$-glucosidase inhibitors, the active compound was found in a methanol extract of Burthus martensi Kirsch. The separation of the active compound was performed using various chromatography methods and the physico-chemical properties of the purified compound were characterized. The compound showed very potent inhibitory activity against ${\alpha}-glucosidase$ with an $IC_{50}$ value of $5.3\;{\mu}g/ml$. Lineweaver-Burk plot indicated that its inhibition of ${\alpha}-glucosidase$ was competitive.

• Journal of Microbiology and Biotechnology
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• v.16 no.12
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• pp.2000-2003
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• 2006

A gene (GenBank AF096282) coding for a $\alpha$-glucosidase (TcaAG, EC 3.2.1.20) from Thermus caldophilus GK24 was expressed in Saccharomyces cerevisiae, a generally recognized as safe (GRAS) host. The thermostable $\alpha$-glucosidase was produced inside of the GRAS host at 0.04 unit/mg-dry cell by the constitutively expressing ADH1 promoter and at 1.2 unit/mg-dry cell by the inductively expressing GALl0 promoter, respectively. No $\alpha$-glucosidase activities were found in the medium when the MF-alpha signal sequence from S. cerevisiae or $\alpha$-amylase signal sequence from Aspergillus oryzae were fused before the $\alpha$-glucosidase gene for the secretion.

• Microbiology and Biotechnology Letters
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• v.42 no.3
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• pp.219-224
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• 2014

In order to develop a new anti-diabetic ${\alpha}$-glucosidase inhibitor, we compared the ${\alpha}$-glucosidase inhibitory activity of the cell-free extracts of 48 strains of yeasts isolated from Korean fermented foods, and found that Pichia burtonii Y257-7 exhibited the highest ${\alpha}$-glucosidase inhibitory activity of 55.6%. The ${\alpha}$-glucosidase inhibitor was maximally produced when Pichia burtonii Y257-7 was cultured in LB broth (initial pH of 6.0) at $28^{\circ}C$ for 24 h. The ${\alpha}$-glucosidase inhibitor, partially purified by Sephadex G-50 gel permeation chromatography and systematic solvents extraction, revealed potent hypoglycemic effects in normal rats and streptozotocin-induced diabetic rats after the oral administration of starch.

• The Korean Journal of Mycology
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• v.43 no.3
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• pp.174-179
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• 2015

For development a new anti-diabetic compound from edible mushroom, antihyperglycemic ${\alpha}$-glucosidase inhibitory activities of Pleurotus ostreatus, Pleurotus cornucopiae, Pleurotus salmoneostramineus, Pleurotus eryngii and Neolentinus lepideus were investigated on its water and ethanol extracts. ${\alpha}$-Glucosidase inhibitory activity of Neolentinus lepideus fruiting body showed the highest at 86.3% in the 95% ethanol extracts and water extract from Pleurotus cornucopiae was also higher at 48.5% among water extracts. Therefore, Neolentinus lepideus which showed very high ${\alpha}$-glucosidase inhibitory activity was selected as a new anti-diabetic agent-containing mushroom and the ${\alpha}$-glucosidase inhibitor was maximally extracted when treated with 95% ethanol at $30^{\circ}C$ for 48 hr. The ethanol extracts from Neolentinus lepideus fruiting body showed dosage-dependent hypoglycemic action after administration to 120 min in the SD-rat and streptozotocin-induced diabetic SD-rat.

• Preventive Nutrition and Food Science
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• v.22 no.3
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• pp.166-171
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• 2017

In this study, we investigated whether Sargassum yezoense extract (SYE) could inhibit ${\alpha}-glucosidase$ and ${\alpha}-amylase$ activities, and alleviate postprandial hyperglycemia in streptozotocin (STZ)-induced diabetic mice. Freeze-dried S. yezoense was extracted with 80% ethanol and concentrated for use in this study. The hypoglycemic effect was determined by evaluating the inhibitory activities of SYE against ${\alpha}-glucosidase$ and ${\alpha}-amylase$ as well as its ability to decrease postprandial blood glucose levels. The half-maximal inhibitory concentrations of SYE against ${\alpha}-glucosidase$ and ${\alpha}-amylase$ were $0.078{\pm}0.004$ and $0.212{\pm}0.064mg/mL$, respectively. SYE was a more effective inhibitor of ${\alpha}-glucosidase$ and ${\alpha}-amylase$ activities than the positive control, acarbose. The increase in postprandial blood glucose levels was significantly alleviated in the SYE group compared with that in the control group of STZ-induced diabetic mice. Furthermore, the area under the curves significantly decreased with SYE administration in STZ-induced diabetic mice. These results suggest that SYE is a potent inhibitor of ${\alpha}-glucosidase$ and ${\alpha}-amylase$ activities and alleviates postprandial hyperglycemia caused by dietary carbohydrates.

• YAKHAK HOEJI
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• v.53 no.3
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• pp.114-118
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• 2009

Bioemulsifiers are those chemicals which are produced from microorganisms but which have both hydrophilic and hydrophobic groups. $\alpha$-Glucosidase inhibitor ($\alpha$-GI) produced from Bacillus lentimorbus B-6 (B-6) showed bioemulsifying activity. But $\beta$-glucosidase inhibitor produced from B-6 didn't show emulsifying activity. $\alpha$-GI was purified from supernatant of B-6 grown in minimal culture medium containing glucose and sodium glutamate by Sephadex G-100 column chromatography and isolated from $\beta$-GI by dialysis against water. Toluene was determined as the best substrate for emulsifying activity of $\alpha$-GI. $\alpha$-GI showed thermostability at $100^{\circ}C$ for 15 min, high salt tolerance up to 32% NaCl and wide range of pH-stability at pH $4\sim10$. Emulsifying character of $\alpha$-GI can be useful for the liposome formation for the treatment of diabetes mellitus.