• Title/Summary/Keyword: ${\alpha}$-Glucosidase

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Inhibitory Effects of Ginseng Seed Oil on α-Glucosidase and α-Amylase Activity (인삼종자오일의 α-Glucosidase 및 α-Amylase 저해작용)

  • Ahn, Chang Ho;Nam, Yun Min;Kim, Shin Jung;Yang, Byung Wook;Kim, Hyoung Chun;Ko, Sung Kwon
    • Korean Journal of Pharmacognosy
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    • v.47 no.1
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    • pp.24-28
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    • 2016
  • This study was to evaluate the effect of ginseng (Panax ginseng) seed oil on the ${\alpha}$-glucosidase and ${\alpha}$-amylase. Each ginseng seed oils (HE, SE, EE) exhibited a significant inhibitory effect (p<0.001) at all concentrations (10 and 20 mg/ml) on ${\alpha}$-glucosidase activity. HE is the highest inhibitory activity (86.92%) at a concentration of 20 mg/ml, SE and EE showed an inhibitory effect of 77.13% and 65.83%, respectively. And also, Each ginseng seed oils (HE, SE, EE) exhibited a significant inhibitory effect (p<0.001) at all concentrations (1 and 2 mg/ml) on ${\alpha}$-amylase activity. HE is the highest inhibitory activity (89.68%) at a concentration of 2 mg/ml, SE and EE showed an inhibitory effect of 76.99% and 65.70%, respectively.

Inhibitory Effects of Proanthocyanidin Extracted from Distylium racemosum on ${\alpha}-Amylase$ and ${\alpha}-Glucosidase$ Activities (조록나무 Proanthocyanidin의 ${\alpha}-Amylase$${\alpha}-Glucosidase$에 대한 저해 효과)

  • Ahn, Jin-Kwon;Park, Young-Ki;Park, So-Young;Kim, Yong-Mu;Rhee, Hae-Ik;Lee, Wi-Young
    • Korean Journal of Pharmacognosy
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    • v.35 no.4 s.139
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    • pp.271-275
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    • 2004
  • Distylium racemosum Sieb. Et Zucc contains some compounds inhibit -amylase activity in experimental conditions. The inhibitory test showed that 50% acetone extracts from the bark and leaves of the plant strongly inhibited salivary -amylase activity. Proanthocyanidin(PA) which has strong inhibitory activity was extracted from the leaves by chromatography on Sephadex LH-20. The inhibitory activities and the inhibition kinetics of the PA were studied against three kinds of enzymes: human salivary ${\alpha}-Amylase$ (SAA), pork pancreatin ${\alpha}-Amylase$ (PAA) and yeast ${\alpha}-Glucosidase$ (AG). Then the activities of PA against SAA, PAA and AG were compared with those of acarbose, a commercial agent. The inhibitory activities of PA were stronger than those of acarbose. Inhibition kinetics of the PA showed competitive inhibition for SAA and PAA, and non competitive inhibition for GA.

Inhibitory Effect of Aqueous Extracts from the Fruit Body of Lentinus edodes on Rat Intestinal Mucosa $\alpha$-glucosidase Activity and Reducing the Increase of Blood Glucose after Streptozotocin-induced Diabetic Rats

  • Lee, In-Soon;Chae, Heui-Jun;Moon, Hae-Yeon
    • Biomedical Science Letters
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    • v.14 no.1
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    • pp.63-68
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    • 2008
  • The aqueous extract from the fruit body of Lentinus edodes was evaluated for inhibitory activities against $\alpha$-glucosidase isolated from Spargue-Dawley male rats. A aqueous extract of Lentinus edodes exhibited 13.8% inhibitory activity on using 2 mM p-nitrophenyl $\alpha$-D-glucopyranoside as a substrate ($IC_{50}$ 75.3 mg/ml). The aqueous extract of Lentinus edodes inhibition type on $\alpha$-glucosidase was determined to be competitive inhibition. When it was oral administered to increase of blood glucose levels after STZ-induced in a dose dependent dietary. These results suggest that aqueous extract of Lentinus edodes effect a metabolism of intestine, and thereby reducing the increase of blood glucose after STZ-induced.

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$\alpha$-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
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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.

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Screening of $\alpha$-amylase and $\alpha$-glucosidase Inhibitors from Brazilian Plant Extracts for Treatment of Rumen Acidosis (100종 브라질 식물 추출물로부터 반추동물 산독증 예방치료를 위한 $\alpha$-amylase 및 $\alpha$-glucosidase 저해제의 선별)

  • Kim, Mi-Sun;An, Seon-Mi;Jung, In-Chang;Kwon, Gi-Seok;Sohn, Ho-Yong
    • Food Science and Preservation
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    • v.17 no.2
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    • pp.290-296
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    • 2010
  • To develop anti-acidosis and anti-diabetes agentsfrom natural products, the inhibitory activities of Brazilian plant extracts against microbial $\alpha$-amylase and $\alpha$-glucosidase were evaluated. Among 100 different ethanol extracts tested, those of Acacia jurema Mart., Anacardium humile A. St.-Hil., Cedrela odorata L., and Guazuma ulmifolia Lam showed good inhibitoryactivities toward both enzymes. In addition, an extract of Plumeria drastica Mart. showed specific inhibition of $\alpha$-amylase, whereas that of Eugenia uniflora L. demonstrated strong inhibition of the enzyme. IC50 values of $\alpha$-amylase inhibition suggested that the extract of A. humile A. St.-Hil., which has been used as an anti-diabetes medicine in Brazil, had potent inhibitory activity. The IC50 for the A. humile A. St.-Hil. extract ($91.2{\mu}g/mL$) was similar to that of acarbose ($50.5{\mu}g/mL$). This activity of A. humile A. St.-Hil. was not reduced by heat or acid treatment. Moreover, treatment with HCl (0.01 M) for 1 h increased the inhibitory activity from 57.5% to 81.2%. Also, the extract did not cause hemolysis of human red blood cells at levels up to 1 mg/mL. The results indicate that the extract of A. humile A. St.-Hil. is potentially useful as an anti-acidosis and anti-diabetes agent.

Screening of α-Amylase, α-Glucosidase and Lipase Inhibitory Activity with Gangwon-do Wild Plants Extracts (강원도 자생 산채 추출물의 α-Amylase, α-Glucosidase, Lipase 효소 저해활성 탐색)

  • Kim, Hee-Yeon;Lim, Sang-Hyun;Park, Yu-Hwa;Ham, Hun-Ju;Lee, Kwang-Jae;Park, Dong-Sik;Kim, Kyung-Hee;Kim, Song-Mun
    • Journal of the Korean Society of Food Science and Nutrition
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    • v.40 no.2
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    • pp.308-315
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    • 2011
  • We investigated ${\alpha}$-amylase, ${\alpha}$-glucosidase and lipase inhibitory activity of extracts collected from wild plants in Gangwon-do. 90 wild plants were collected and their water and ethanol extracts were obtained. Results of measuring ${\alpha}$-amylase inhibitory activity indicated more than 80% of activity inhibition in 10 mg/mL concentration for ethanol extracts of three plants and water extracts of two plants. For ${\alpha}$-glucosidase inhibitory activity, ethanol extracts of thirteen plants and water extracts of three plants showed more than 80% of activity inhibition in 10 mg/mL concentration. In the experiment of inhibiting lipase activity, ethanol extracts of seven plants and water extracts of one plants showed above 80% of activity inhibition in 10 mg/mL concentration. These results suggest that the selected extracts could be potentially used as a resource of bioactive materials for health functional foods.

α-Glucosidase Inhibitory Effect of Vicine and α-Eleostearic Acid from the Seeds of Momordica charantia (여주씨에서 분리한 Vicine과 α-Eleostearic Acid의 α-glucosidase 저해효과)

  • Yuk, Heung Joo;Noh, Geon Min;Choe, Jeong Sook;Kwon, Oh Kyung;Hong, Su Young;Kang, Sang Soo;Cho, Kye Man;Park, Dong Sik
    • Korean Journal of Environmental Agriculture
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    • v.34 no.1
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    • pp.57-63
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    • 2015
  • BACKGROUND: Momordica charantia (MC) have been used in various parts of the world to treat diabetes. Despite the highest effects of phytochemicals than any other part of the plant, the main components of seed of MC grown in Korea and their properties have not been studied extensively. METHODS AND RESULTS: The seeds of MC were extracted into five different polarity solvents: 30%, 50%, 70%, 95% ethanol and distilled water. The 95% ethanol extract showed the most potent inhibition ($IC_{50}=88.7{\mu}g/mL$) against ${\alpha}$-glucosidase. To investigate the compounds responsible for this effect, activity guided fractionation of MC seeds by chromatography yielded two phytochemicals which were confirmed as vicine (1) and ${\alpha}$-eleostearic acid (2) based on their NMR and ESI-MS spectroscopic data. Among them, ${\alpha}$-eleostearic acid (2) possessed potent ${\alpha}$-glucosidase inhibitory activities with $IC_{50}$ values from $32.4{\mu}g/mL$. CONCLUSION: Collectively, the results from this present study strongly suggest that both extract and ${\alpha}$-eleostearic acid (2) have potent ${\alpha}$-glucosidase inhibitory activity. Furthermore, ${\alpha}$-eleostearic acid (2) as the most active ${\alpha}$-glucosidase inhibitor was proven to be present in high quantities in the MC seeds by a HPLC chromatogram.

Linoleic Acid from Bamboo (Phyllostachys Bambusoides) Displaying Potent α- Glucosidase Inhibition (대나무로부터 분리한 linoleic acid의 α-glucosidase 저해활성 연구)

  • Jung, Sun-In;Kang, Su-Tae;Choi, Cheol-Yong;Oh, Kyeong-Yeol;Cho, Jung-Keun;Rengasamy, Rajesh;Park, Ki-Hun
    • Journal of Life Science
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    • v.19 no.5
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    • pp.680-683
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    • 2009
  • Glycosidase inhibitors are major targets in the treatment of type II diabetes, cancer and viral infections. This study was carried out to investigate the glycosidase inhibitory substances from bamboo (Phyllostachys bambusoides). Bamboo was extracted with methanol and then further fractionated with n-hexane, chloroform, n-BuOH and aqueous to get an active fraction. All extracts were evaluated for ${\alpha}$-glucosidase inhibitory activities to identify the n-hexane fraction with 33.5 ${\mu}$g/ml of IC50 value. Active compound 1 in the n-hexane fraction was identified as linoleic acid, which exhibited inhibitory activity with 12.4 ${\mu}$M of IC50 value. Mechanistic analysis showed that linoleic acid exhibited noncompective inhibition. This is the first study in which bamboo is reported to show ${\alpha}$-glucosidase inhibitory activity.

Free radical scavenging and α-glucosidase inhibitory effects of a roots extract of Aruncus dioicus var. kamtschaticus (재배 삼나물 뿌리 추출물의 자유 라디칼소거 및 α-glucosidase 저해활성)

  • Jeong, Gyeong Han;Kim, Tae Hoon
    • Food Science and Preservation
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    • v.23 no.7
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    • pp.989-994
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    • 2016
  • As part of our continuing search for bioactive natural products, the antioxidant and ${\alpha}$-glucosidase inhibitory activities of an 80% methanolic extract and organic solvent soluble-portions of Aruncus dioicus var. kamtschaticus roots were investigated by using a bioassay system. The antioxidant activity of A. dioicus var. kamtschaticus roots extract and organic solvent soluble-portions were assessed by examining with 1,1-diphenyl-2-picrylhydrazyl (DPPH) and 2,2'-azino-bis (3-ethylbenzothiazoline-6-sulphonic acid) ($ABTS^+$) radical scavenging. In addition, anti-diabetic effects of the A. dioicus var. kamtschaticus root extract and organic solvent soluble-portions were tested via ${\alpha}$-glucosidase inhibition assay. The total phenolic contents of the products were determined by applying UV-VIS spectrophotometry. All tested samples showed dose-dependent radical scavenging and ${\alpha}$-glucosidase inhibitory properties. In particular, the ${\alpha}$-glucosidase inhibitory and radical scavenging effects of the ethyl-acetate (EtOAc)-soluble portion from the roots of A. dioicus var. kamtschaticus were greater than those from other solvent-soluble portions. These results indicate that A. dioicus var. kamtschaticus could be considered a new effective source of natural antioxidants and anti-diabetic materials. More systematic research of the constituents of the roots of this A. dioicus variety will be conducted to further develop its antioxidative and anti-diabetic properties.

Characteristics of Cellulomonas fimi $\beta$-glucosidase expressed in Escherichia coli (대장균에서 발현되는 Cellulomonas fimi $\beta$-glucosidase의 효소학적 특징)

  • Kim, Ha-Kun
    • The Journal of Natural Sciences
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    • v.8 no.2
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    • pp.57-61
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    • 1996
  • The $\beta$-glucosidase enzyme was purified from E. coli carrying Cellulomonas fimi $\beta$-glucosidase gene. SDS-PAGE and analytical gel filtration revealed that molecular weight of this enzyme was 56,000 dalton and consisted of a single polypeptide.Inhibition caused by heavy metals and activation by dithiothreitol suggest the existence of essential thiol group in the enzyme. The enzyme was not active on maltose (glucose $\alpha$-1,4-glucose) which has a $\alpha$-linkage, whereas it was active on lactose (glucose $\beta$-1,4-glucose), PNPG (p-nitrophenyl $\beta$-D-glucopyranoside) and PNPC (p-nitrophenyl $\beta$-D-cellobioside), although its reaction rates were different.

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