• Journal of Microbiology and Biotechnology
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• v.12 no.6
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• pp.895-900
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• 2002

A soil microorganism producing ${\alpha}$- and ${\beta}$-glucosidase inhibitors was identified as Bacillus lentimorbus, based on the fatty acid and morphological analyses, along with biochemical and physiological tests. The ${\alpha}$-glucosidase inhibitor was highly produced by this strain in a culture medium containing $0.25\%$ of sodium glutamate and $0.5\%$ of glucose, pH 8.0 at $30^{\circ}C$ for 2 days. The ${\alpha}$-glucosidase inhibitor from culture filtrate of his strain was identified as water soluble, organic solvent nonextractable, and heat stable. In addition to ${\alpha}$-glucosidase inhibitor, this strain also produced ${\beta}$-glucosidase inhibitor in he same culture medium and this inhibitor showed an antifugal activity against Botrytis cinerea. While the production of ${\alpha}$- glucosidase inhibitor was decreased by a glucose concentration higher than $1\%$, the production of ${\beta}$-glucosidase inhibitor was lot Influenced by a glucose concentration higher than $20\%$. The ${\alpha}$-glucosidase inhibitor from culture filtrate of this strain was separated from the ${\beta}$-glucosidase inhibitor through Sephadex G-100 column chromatography.

• Journal of Microbiology
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• v.42 no.3
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• pp.223-227
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• 2004

An ${\alpha}$-glucosidase inhibitor, SKG-3, was isolated from the fruiting bodies of Ganoderma lucidum and its physico-chemical properties were characterized. It was a highly specific and effective reversible inhibitor of ${\alpha}$-glucosidase. It showed very potent inhibitory activity against a-glucosidase with an IC$\sub$50/ value of 4.6$\mu\textrm{g}$/$m\ell$, but no activity for any other glycosidases tested. Enzyme activity could be recovered upon dialysis, thus providing evidence for the reversibility of the inhibition. A Lineweaver-Burk plot indicated that the SKG-3 inhibition of ${\alpha}$-glucosidase was competitive.

• Microbiology and Biotechnology Letters
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• v.18 no.1
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• pp.39-43
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• 1990

The inhibitor had the inhibitory activities against hydrolysis of PNPG, sucrose and ONPG by $\alpha$-Dglucosidase, $\alpha$ - and $\beta$ -galactosidase, but it did not inhibit amylases and other carbohydrases. Kinetic studies exhibited that the inhibitory substance non-competitively inhibited the enzyme reaction with a Ki value of 118 $\mu$g/m$\ell$, and enzyme-inhibitor complex was formed slowly.

• Microbiology and Biotechnology Letters
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• v.17 no.3
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• pp.202-206
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• 1989

A microorganism, YS-221-B strain which powerfully produced $\alpha$-D-Glucosidase Inhibitor was isolated from soil. The morphological, cultural characteristics and physiological properties of the strain were investigated. As the results of various examinations, the strain YS-221-B was identified to be similar to Streptomyces flavouirens except the utilization of raffinose, i-inositol among the various carbon sources.

• Journal of Microbiology and Biotechnology
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• v.25 no.2
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• pp.174-177
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• 2015

A potent α-glucosidase inhibitor (compound I) was isolated from coffee brews by activity-based fractionation and identified as a β-carboline alkaloid norharman (9H-pyrido[3.4-b]indole) on the basis of mass spectroscopy and nuclear magnetic resonance spectra (¹H NMR, ¹³C NMR, and COSY). The norharman showed potent inhibition against α-glucosidase enzyme in a concentration-dependent manner, with an IC₅₀ value of 0.27 mM for maltase and 0.41 mM for sucrase. A Lineweaver-Burk plot revealed that norharman inhibited α-glucosidase enzyme uncompetitively, with a K_i value of 0.13 mM.

• Korean Journal of Microbiology
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• v.50 no.4
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• pp.381-383
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• 2014

In the course of screening for ${\alpha}$-glucosidase inhibitor produced by microorganism, the active compound was isolated from the culture filtrate of Bacillus sp. SKU31-1 using a series of chromatography procedures. The structure of the active compound was elucidated as 5-amino-1-hydroxymethyl-1, 2, 3, 4-cyclohexanetetrol on the basis of spectroscopic evidence obtained and comparison with data from the literature. The active compound showed potent inhibitory activity against ${\alpha}$-glucosidase with an $IC_{50}$ value of $1.9{\mu}M$ for maltose and 4.9 mM for sucrose. A Lineweaver-Burk plot indicated that its inhibition of ${\alpha}$-glucosidase was competitive, with a $K_i$ value of 0.15 mM.

• Mycobiology
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• v.41 no.3
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• pp.149-154
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• 2013

An ${\alpha}$-glucosidase inhibitor was developed from Aspergillus oryzae N159-1, which was screened from traditional fermented Korean foods. The intracellular concentration of the inhibitor reached its highest level when the fungus was cultured in tryptic soy broth medium at $27^{\circ}C$ for five days. The inhibitor was purified using a series of purification steps involving ultrafiltration, Sephadex G-25 gel permeation chromatography, strong cation exchange solid phase extraction, reverse-phase high performance liquid chromatography, and size exclusion chromatography. The final yield of the purification was 1.9%. Results of the liquid chromatography-tandem mass spectrometry (LC-MS/MS) analysis indicated that the purified ${\alpha}$-glucosidase inhibitor was a tri-peptide, Pro-Phe-Pro, with the molecular weight of 360.1 Da. The IC50 value of the peptide against ${\alpha}$-glucosidase activity was 3.1 mg/mL. Using Lineweaver-Burk plot analysis, the inhibition pattern indicated that the inhibitor acts as a mixed type inhibitor.

• Microbiology and Biotechnology Letters
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• v.17 no.5
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• pp.529-532
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• 1989

A strain of Streptomyces sp. (YS-221-B) extracellularly produced an inhibitory substance for $\alpha$-D-Glucosidase. The substance was purified 96-fold from culture filtrate by dialysis, heat treatment, adsorption on active carbon, Bio-Gel P-10 and Sephadex G-75 column chromatography with yield of 9.2%. The substance was stable in pH range from 7.0 to 11.0 at 37$^{\circ}C$, and a treatment at 10$0^{\circ}C$ for 20 min diminished only 15% of the original activity. The inhibitor was not inactivated by the treatment of $\alpha$-, $\beta$-amylases, glucoamylases, trypsin and chymotrypsin but inactivated by pyoteases from Streptomyces griseus and Tritirachium album.

• Korean Journal of Pharmacognosy
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• v.31 no.2
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• pp.196-202
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• 2000

This study was conducted to search for the ${\alpha}-glucosidase$ inhibitor from the natural products. In the previous study, the water extract of Gyrophora esculenta exhibited a potent inhibitory effect on ${\alpha}-glucosidase$ activities. Then, by bioassay-guided fractionation followed by chromatographic separation of the water extract of Gyrophora esculenta, ${\alpha}-glucosidase$ inhibitor was isolated as GE974. GE974 showed significant inhibitory activities on some kinds of ${\alpha}-glucosidase$ in vitro. Its inhibitory mechanism seemed to be competitive for disaccharides. Also, it markedly inhibited ${\alpha}-glucosidases$ of intestine separated from both nondiabetics and diabetics.

• Microbiology and Biotechnology Letters
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• v.44 no.2
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• pp.124-129
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• 2016

The extraction and purification of the anti-hyperglycemic α-glucosidase inhibitor from an edible mushroom, Pleurotus cornucopiae, were investigated. The inhibitor was maximally extracted when the P. cornucopiae fruiting body was treated with distilled water at 30℃ for 12 h. Purification was achieved using Sephadex G-100 and G-50 filtration chromatography, pepsin hydrolysis, and reverse-phase HPLC. The compound’s solid yield and inhibitory activity were 12.2% and 9.10 mg/ml of IC₅₀, respectively. The purified inhibitor contained two hexapeptides with Thr-Ile-Ala-Phe-Ile-Asp (A) and Tyr-Tyr-Ala-Ile-Gly-Asp (B) sequences and molecular weights of 678.79 Da (A) and 643.7 Da (B). The purified inhibitor showed a mixed inhibition pattern to α-glucosidase and a dose-dependent anti-hyperglycemic effect in a streptozotocininduced diabetic Sprague-Dawley rat model, exhibited by decreased blood glucose levels at doses of 50 and 300 mg/kg.