• 제목/요약/키워드: -glucosidase

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당 분해효소를 이용한 백하수오 뿌리로부터 분리한 Pregnane Glycosides의 생전환 (Biotransformation of Pregnane Glycosides from Cynanchum wilfordii Roots by β-Glucosidase)

  • 윤미영;끄엉 마이뉴엔;최경자;최용호;장경수;차병진;김진철
    • 식물병연구
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    • 제18권3호
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    • pp.186-193
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    • 2012
  • 생물전환은 친환경적이며 생물이용성을 증가시킬 수 있는 효과적인 방법이다. 백하수오 추출물을 이용해 보리 흰가루병에 대한 항균활성을 증진시키기 위하여 본 연구자들은 ${\beta}$-glucosidase를 이용하여 wilfoside C1G의 생물전환을 수행하였다. Wilfoside C1G와 cynauricuoside A(K1G)가 포함된 G 시료로부터 glucopyranosyl moiety를 분해하기 위하여 ${\beta}$-glucosidase를 처리하였다. 효소반응을 통해 wilfoside C1G와 K1G는 각각 wilfoside C1N과 wilfoside K1N으로 완전히 전환되었다. G 시료를 이용한 생물전환의 최적 조건은 에탄올 10%, 1,555 ${\mu}U$ ${\beta}$-glucosidase/ml, pH 5 및 $45^{\circ}C$로 결정되었다. 최적조건을 통해 생물전환을 실시한 후 흰가루병에 대한 방제효과를 조사한 결과, ${\beta}$-glucosidase에 의해 생물전환된 G 시료는 ${\beta}$-glucosidase가 처리되지 않은 G 시료보다 보리 흰가루병에 대해 우수한 방제효과를 나타냈다. 따라서 ${\beta}$-glucosidase를 이용한 생물전환은 흰가루병 방제 효과가 있는 백하수오 추출물의 항균활성을 증가시키는데 유용한 기술로 적용이 가능할 것으로 추정된다.

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

  • Kim, Shin-Duk;Nho, Hong Joon
    • Journal of Microbiology
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    • 제42권3호
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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.

Effect of Paeonia lactiflora Extracts on ${\alpha}-Glucosidase$

  • Lee, Sung-Jin;Ji, Seung-Tack
    • Natural Product Sciences
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    • 제10권5호
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    • pp.223-227
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    • 2004
  • This study was carried out to investigate inhibitory effect of extracts from the root of Paeonia lactiflora on postprandial hyperglycemia. Organic solvent (hexane, ethyl acetate, butanol, aqueous) extracts from the crude drug were fractionated by high performance liquid chromatography. These fractions were examined to evaluate ${\alpha}-glucosidase$ (EC 3. 2. 1. 20) inhibition by microplate colorimetric assay. Among the fractions examined, the ethyl acetate fraction from the roots of Paeonia lactiflora showed potent inhibitory effects on ${\alpha}-glucosidase$. Therefore, further fractionation of the fraction was carried out to isolate the active principles. Finally, we isolated and Purified 1,2,3,4,6-penta-O-galloyl-beta-D-glucose (PGG) as a active principle by activity-guided fractionation. These results suggest that the extract from the root of Paeonia lactiflora can be used as a new nutraceutial for inhibition on postprandial hyperglycemia and PGG might be a candidate for developing an ${\alpha}-glucosidase$ inhibitor.

Expression of Thermostable $\alpha$-Glucosidase from Thermus caldophilus GK24 in Recombinant Saccharomyces cerevisiae

  • Choi, Jae-Youl;Ahn, Jung-Oh;Kim, Sun-Il;Shin, Hyun-Jae
    • Journal of Microbiology and Biotechnology
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    • 제16권12호
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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.

Pseudomonas sp. 유래 Endo-1,4-$\beta$-Glucanase 및$\beta$-1,4-Glucosidase 유전자의 안정성 개선 (Enhanced stability of Pseudomonas sp. Endo-1,4-$\beta$$\beta$-1,4-Glucosidase Gene)

  • 김양우;전성식;정영철;노종수;성낙계
    • 한국미생물·생명공학회지
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    • 제23권6호
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    • pp.659-664
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    • 1995
  • To improve stability of recombinant DNA pLC1 encoding endoglucanase gene and pGL1 encoding $\beta $-glucosidase gene, DNA fragments of genes coding endoglucanase and $\beta $-glucosidase were cloned within the recA gene on a pDR1453, and the pDRE10 and pDRG20 of recombinant plasmids were integrated into the recA gene on the E. coli 1100 chromosomal DNAs. The stability of inheritance was completely maintained in E. coli 1100; Transformants E. coli 1100/pDREIO and pDRG20 were expressed well by recA promoter and increased endoglucanase and $\beta $-glucosidase activities. This method can be used as a model to improve the stability of recombinant plasmid in large scale culture.

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

  • 도재호;주현규
    • 한국미생물·생명공학회지
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    • 제18권1호
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    • pp.39-43
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    • 1990
  • 본 저해물질은 10Mug의 Alpha-D-glucosidase에 대해서 50Mug 및 100Mug을 첨가했을 때 저해율은 각각 60, 80 정도였으며 enzyme-inhibitor complex를 비교적 서서히 형성하여 5분간 진처리하였을 때 약 55의 저해율을 나타내었다. 그리고 Alpha-D-glucosidase, Alpha-galactosidase및 Beta-galactosidase를 제외한 탄수화물 분해효소에 대해서는 저해능이 없었으며, Alpha-D-glucosidase에 대한 저해양상은 non-competitive type 이었으며 Ki 값은 118 $\mu$g/m$\ell$였다.

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갈근에서 분리한 화합물의 $\alpha$-glucosidase와 $\alpha$-amylase 활성 저해 효과 ($\alpha$-Glucosidase and $\alpha$-Amylase Inhibitory Activity of Compounds from Roots Extract of Pueraria thunbergiana)

  • 박지희;백목련;이병회;연규환;유시용;김영섭;박상언;홍경식
    • 한국약용작물학회지
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    • 제17권5호
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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.

마전자 추출물의 항산화 및 Alpha-Glucosidase 저해 활성 (Antioxidant and Alpha-Glucosidase Inhibitory Activity of Strychnos nux-vomica Extracts)

  • 이정민;박재희;박해룡;박은주
    • 한국식품영양과학회지
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    • 제39권9호
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    • pp.1243-1248
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    • 2010
  • 본 연구는 마전자(Strychnos nux-vomica) 추출물의 항산화 활성 및 $\alpha$-glucosidase 저해활성을 측정하였다. 먼저, 마전자를 각각의 용매로 추출하여 페놀 함량을 알아본 결과 100 g당 SNM에서 71.43 mg을 함유하고 있으며, SNE에서는 24.51 mg, SNA에서는 11.17 mg을 함유하고 있었다. DPPH 라디칼 소거능은 SNM, SNE가 1 mg/mL의 농도에서 50% 정도의 활성을 나타내 항산화 효과가 있다는 것을 확인할 수 있었다. 또한 $200\;{\mu}M$ $H_2O_2$에 의한 DNA 손상에 대해 마전자 추출물의 보호 효과를 확인할 수 있었다. SNM의 $\alpha$-glucosidase 저해활성 측정 시 SNM 1 mg/mL의 농도에서 12.8%의 억제 활성을 나타내었고, SNM 처리시간을 증가시킬 경우 그 활성도가 유의적으로 증가하는 것을 보였다. 이상의 결과로 마전자 추출물의 항산화 활성 및 SNM의 $\alpha$-glucosidase 억제 활성을 확인할 수 있었다.

화살나무(Euonymus alatus)로 부터 α-glucosidase 저해 물질의 분리 및 동정 (Isolation and Characterization of α-glucosidase Inhibitors from Euonymus alatus)

  • 김신덕
    • 한국미생물·생명공학회지
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    • 제45권4호
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    • pp.311-315
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    • 2017
  • 화살나무 가지로부터 activity based fractionation에 의해 ${\alpha}$-glucosidase 저해 활성 물질 compound 1-4을 분리하였고, $^1H$ NMR, $^{13}C$ NMR, $^1H-^1H$ COSY와 HMBC 등의 spectral data에 의해 구조를 결정하였다. Compound 1-4는 모두 flavonol 물질로 ${\alpha}$-glucosidase에 대해 $IC_{50}$ 값이 각각 25.3, 17.1, 47.3과 $35.1{\mu}M$로 positive control로 사용한 acarbose 보다 강한 활성을 나타내었다. 화살나무의 혈당 저하 기능의 유효성분으로 처음 동정된 Compound 1-4는 ${\alpha}$-glucosidase에만 특이적 활성을 갖는 물질로 당뇨병 치료제로의 개발 가능성이 높은 물질로 사료된다.

Enhancement of ${\beta}$-Glucosidase Activity from a Brown Rot Fungus Fomitopsis pinicola KCTC 6208 by Medium Optimization

  • Park, Ah Reum;Park, Jeong-Hoon;Ahn, Hye-Jin;Jang, Ji Yeon;Yu, Byung Jo;Um, Byung-Hwan;Yoon, Jeong-Jun
    • Mycobiology
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    • 제43권1호
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    • pp.57-62
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    • 2015
  • ${\beta}$-Glucosidase, which hydrolyzes cellobiose into two glucoses, plays an important role in the process of saccharification of the lignocellulosic biomass. In this study, we optimized the activity of ${\beta}$-glucosidase of brown-rot fungus Fomitopsis pinicola KCTC 6208 using the response surface methodology (RSM) with various concentrations of glucose, yeast extract and ascorbic acid, which are the most significant nutrients for activity of ${\beta}$-glucosidase. The highest activity of ${\beta}$-glucosidase was achieved 3.02% of glucose, 4.35% of yeast extract, and 7.41% ascorbic acid where ascorbic acid was most effective. The maximum activity of ${\beta}$-glucosidase predicted by the RSM was 15.34 U/mg, which was similar to the experimental value 14.90 U/mg at the 16th day of incubation. This optimized activity of ${\beta}$-glucosidase was 23.6 times higher than the preliminary activity value, 0.63 U/mg, and was also much higher than previous values reported in other fungi strains. Therefore, a simplified medium supplemented with a cheap vitamin source, such as ascorbic acid, could be a cost effective mean of increasing ${\beta}$-glucosidase activity.