• Journal of Microbiology and Biotechnology
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• 제12권6호
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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.

• 약학회지
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• 제53권3호
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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.

• 한국미생물·생명공학회지
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• 제17권3호
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• pp.202-206
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• 1989

토양으로부터 $\alpha$-D-Glucosidase Inhibitor를 강력히 분비하는 방선균속 균주를 분리한 후 균의 형태학적특성, 배양성 및 생리화학적 특성을 조사하여 동정한 결과 Streptomyces flavovirens 또는 그 근연균으로 동정되었다.

• 한국미생물·생명공학회지
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• 제44권2호
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• pp.124-129
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• 2016

식용버섯인 노랑느타리버섯으로부터 α-glucosidase 저해제의 추출과 정제에 대하여 연구하였다. α-glucosidase 저해제는 노랑느타리버섯 자실체를 증류수로 30℃에서 12시간 처리하였을 때 가장 많이 추출되었다. α-glucosidase 저해제를 sephadex G-100 여과 크로마토그래피와 펩신 가수분해, sephadex G-50 여과 크로마토그래피, 역상 HPLC로 정제한 결과 수율과 α-glucosidase 저해활성은 각각 12.2%와 IC₅₀ 9.10 mg/ml이었다. 정제한 α-glucosidase 저해제는 Thr-Ile-Ala-Phe-Ile-Asp (A)과 Tyr-Tyr-Ala-Ile-Gly-Asp (B)의 서열을 갖고 있는 두개의 헥사펩타이드를 함유하였고 이들의 분자량은 각각 (A)가 678.79 Da, (B)가 643.7 Da이었다. 정제한 α-glucosidase 저해제는 α-glucosidase에 대하여 혼합형 저해양상을 보였고 streptozotocin으로 유도된 당뇨 쥐모델에서 50 mg/kg과 300 mg/kg 투여시 혈당함량을 낮추어 주는, 농도 의존적 혈당상승억제 효과를 보였다.

• Journal of Microbiology and Biotechnology
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• 제25권2호
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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.

• 한국미생물·생명공학회지
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• 제17권5호
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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.

• Archives of Pharmacal Research
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• 제20권4호
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• pp.346-350
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• 1997

The synthesis of cis- and trans-1,6-dihydroxypyrrolizidine starting from trans-4-hydroxy-L-proline and their evaluation as glycosidase inhibitors are reported. The cis-isomer was found to be a potent inhibitor against .alpha.-glucosidase and showed weak inhibitory effect against other glycosidases. The trans-isomer exhibited weak inhibitions of b-glucosidase and amylo-glucosidase and poor inhibition of other glycosidases.

• 한국미생물·생명공학회지
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• 제17권3호
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• pp.207-212
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• 1989

토양으로부터 분리 한 균주 YS-221-B로부터 $\alpha$-D-Glucosidase Inhibitor 생산조건을 검토한 결과는 다음과 같다. 최적 pH와 온도는 8.0, 3$0^{\circ}C$였으며, 탄소원으로는 mannitol, 1-Inositol, erythritol과 같은 당알코올이 양호하였으며, 질소원으로는 asparagine, beef extract가 양호하였다. Riboflavin, folic acid, thiamine과 같은 vitamin의 첨가에 의해서 저해물질 생산이 10~20% 증가되었으며, 금속이온 중에 $Zn^{++}$, $Mg^{++}$은 약 20% 정도 물질생산을 촉진시켰으나 Li$^+$, Co$^{++}$ $Ca^{++}$, Fe$^{++}$ 등은 감소시켰다. 그리고 pH8.0, 3$0^{\circ}C$에서 8~9일간 배양함으로써 저해물질 생산이 최고에 달하였다.

• International Journal of Industrial Entomology and Biomaterials
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• 제21권2호
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• pp.163-167
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• 2010

[ $\alpha$ ]Glucosidase (EC 3.2.1.20) is a glycosidase that hydrolyzes disaccharides, oligosaccharides, and polysaccharides resulting in the release of α-D-glucose. In this study, $\alpha$-glucosidase activity in the hemolymph and midgut of the mulberry silkworm Bombyx mori and Japanese oak silkmoth Antheraea yamamai was measured using maltose, sucrose, trehalose, and p-nitrophenyl $\alpha$-D-glucopyranoside as substrates. In general, hemolymph $\alpha$-glucosidase activity was higher in B. mori than in A. yamamai. In contrast, midgut $\alpha$-glucosidase activity was higher in A. yamamai than in B. mori for all of the substrates tested. $\alpha$-Glucosidase activity in the midgut of both B. mori and A. yamamai showed similar responses to changes in pH and temperature for all of the substrates tested. Native (7.5%) PAGE of hemolymph and midgut proteins from B. mori and A. yamamai followed by staining with 4-methylumbelliferyl $\alpha$-D-glucoside (MUG) indicated that the $\alpha$-glucosidases of these related lepidopterans are functionally similar but structurally different. In comparison to $\alpha$-glucosidase activity from A. yamamai, $\alpha$-glucosidase activity from B. mori was generally less sensitive to the $\alpha$-glucosidase inhibitors, 1-deoxynojirimycin (DNJ), acarbose, and voglibose when the activity was determined using maltose, sucrose, and trehalose.

• 한국미생물·생명공학회지
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• 제25권2호
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• pp.189-196
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• 1997

A producer of inhibitor against ${\beta}-glucosidase$ of Penicillium sp.-L4 was screened from Actinomycetes, and the isolated strain was identified as Streptomyces sp. The inhibitor produced was very stable against heat, acidic and alkaline conditions, proteolytic and amylolytic enzymes. The inhibotor was purified from culture broth through activated carbon treatment, ultrafiltration, anion and cation exchange, activated carbon columm, acetone precipitation and preparative HPLC. It showed inhibitory activities against a variety of dissacharide hydrolyzing enzymes produced by P.sp.-L4, and the mode of inhibition was competitive. Its structure and molecular formular was elucidated by IR, $^1H\;and\;^{13}C$ NMR and FAB/Mass spectrometry, which was identified as 1-deoxynojirimycin (dNM). dNM showed inhibitory effects on the cell growth and hydrolytic enzyme action of P.sp.-L4 on agar plate and infected lemon peel.