• Title, Summary, Keyword: ${\alpha}$-glucosidase inhibitor

Search Result 96, Processing Time 0.06 seconds

Production of $\alpha$-Glucosidase Inhibitor by $\beta$-Glucosidase Inhibitor-Producing Bacillus lentimorbus B-6

  • Kim, Kyoung-Ja;Yang, Yong-Joon;Kim, Jongkee
    • Journal of Microbiology and Biotechnology
    • /
    • v.12 no.6
    • /
    • pp.895-900
    • /
    • 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.

Inhibition Mechanism of $\alpha$-D-Glucosidase Inhibitor from Streptomyces sp (Streptomyces속 균주가 생성하는 $\alpha$-D-Glucosidase 저해물질의 작용상)

  • 도재호;주현규
    • Microbiology and Biotechnology Letters
    • /
    • v.18 no.1
    • /
    • pp.39-43
    • /
    • 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.

  • PDF

Isolation and Characterization of $\alpha$-Glucosidase Inhibitor from the Fungus Ganoderma lucidum

  • Kim, Shin-Duk;Nho, Hong Joon
    • Journal of Microbiology
    • /
    • v.42 no.3
    • /
    • pp.223-227
    • /
    • 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.

Production and Characterization of a New ${\alpha}$-Glucosidase Inhibitory Peptide from Aspergillus oryzae N159-1

  • Kang, Min-Gu;Yi, Sung-Hun;Lee, Jong-Soo
    • Mycobiology
    • /
    • v.41 no.3
    • /
    • pp.149-154
    • /
    • 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.

Emulsifying Character of $\alpha$-Glucosidase Inhibitor Produced from Bacillus lentimorbus B-6 (Bacillus lentimorbus B-6 균주로부터 생산된 $\alpha$-Glucosidase 억제제의 생물 유화제로서의 특성)

  • Yang, Young-Joon;Kim, Kyoung-Ja
    • YAKHAK HOEJI
    • /
    • v.53 no.3
    • /
    • pp.114-118
    • /
    • 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.

Inhibitory Effect of GE974 isolated from Gyrophora esculenta on ${\alpha}-Glucosidase$ (석이에서 분리한 GE974의 ${\alpha}-Glucosidase$ 저해효과)

  • Choi, Hyuck-Jai;Kim, Dong-Hyun;Kim, Nam-Jae
    • Korean Journal of Pharmacognosy
    • /
    • v.31 no.2
    • /
    • pp.196-202
    • /
    • 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.

  • PDF

$\alpha$-D-Glucosidase Inhibitor from Streptomyces sp. (I) - Identification of the Strain - (Streptomyces속 균주가 생성하는 $\alpha$-D-Glucosidase Inhibitor( I ) -균주의 동정 -)

  • 도재호;주현규
    • Microbiology and Biotechnology Letters
    • /
    • v.17 no.3
    • /
    • pp.202-206
    • /
    • 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.

  • PDF

Isolation and Characterization of α-Glucosidase Inhibitor Produced by Bacillus sp. SKU31-1 Strain (Bacillus sp. SKU31-1가 생산하는 α-Glucosidase 저해제 분리 및 특성 조사)

  • Kim, Shin-Duk
    • Korean Journal of Microbiology
    • /
    • v.50 no.4
    • /
    • pp.381-383
    • /
    • 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.

Polyopes lancifolia Extract, a Potent α-Glucosidase Inhibitor, Alleviates Postprandial Hyperglycemia in Diabetic Mice

  • Min, Seong Won;Han, Ji Sook
    • Preventive Nutrition and Food Science
    • /
    • v.19 no.1
    • /
    • pp.5-9
    • /
    • 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.

$\alpha$-D-Glucosidase Inhibitor from Streptomyces Sp. (III) - Purification and Stability of the Inhibitor - (Streptomyces속 균주가 생성하는 $\alpha$-D-Glucosidase Inhibitor(III) -저해물질의 정제 및 안정성-)

  • 도재호;주현규
    • Microbiology and Biotechnology Letters
    • /
    • v.17 no.5
    • /
    • pp.529-532
    • /
    • 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.

  • PDF