• 제목/요약/키워드: ${\beta},D-glucosidase$

검색결과 89건 처리시간 0.222초

Cloning of $\beta$-glucosidase gene from Cellulomonas sp. into E.coli

  • 김하근;김훈;박무영
    • 한국미생물생명공학회:학술대회논문집
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    • 한국미생물생명공학회 1986년도 추계학술대회
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    • pp.525.1-525
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    • 1986
  • To clone ${\beta}$-glucosidase gene from Cellulomonas sp. a gene library was constructed using E. coli JM83 pUC9. Among 2,500 pseudotransformants obtained, 20 clones developed yellow color on the p-nitrophenyl- -D-glucopyranoside filter paper These 20 clones were classified into three groups based on the results of activity staining using nondenaturating polyacrylamide gel electrophoresis and restriction enzyme digestions. Among the three groups, only one group containing pCEl plasmid has specificity for cellobiose.

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Effects of Dietary Fructan on Cecal Enzyme Activities in Rats

  • Kang, Soon-Ah;Chun, Uck-Han;Jang, Ki-Hyo
    • Biotechnology and Bioprocess Engineering:BBE
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    • 제10권6호
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    • pp.582-586
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    • 2005
  • In this Study, we have attempted to determine the effects of dietary fructose polymers (fructan), high molecular-weight ${\beta}-(2,6)-linked$ levan, and low-molecular-weight ${\beta}-(2,1)-linked$ inulin, on two intestinal enzymes $({\beta}-glucuronidase\;and\;{\beta}-glucosidase)$. As a preliminary experiment, when intestinal microflora were cultured in anaerobic media harboring levan or its oligosaccharides, bacterial cell growth was observed in the levanoligosaccharide-supplemented media, but not in the levan-supplemented media, indicating that levan's size is important for the utilization by intestinal bacteria of levan as an energy Source. In our animal study, the intake of a levan-rich diet was determined to significantly attenuate the activity of the harmful enzyme $({\beta}-glucuronidase$, but d id not affect the activity of ${\beta}-glucosidase$.

안개나무 가지 추출물로부터 분리한 $\alpha$-glucosidase 저해활성물질 (Alpha-glucosidase Inhibitors from the Branches Extract of Cotinus coggygria)

  • 차미란;박지희;최연희;최춘환;홍경식;최상운;김영섭;김영균;김영호;유시용
    • 생약학회지
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    • 제40권3호
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    • pp.229-232
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    • 2009
  • The ethanol (EtOH) extract of the branches of Cotinus coggygria (Anacardiaceae) exhibited a significant inhibition on the yeast $\alpha$-glucosidase, one of the key enzymes related with diabetes mellitus, in a dose dependent manner, in vitro. The intensive phytochemical survey of the EtOH extract of the species by way of bioactivity-guided fractionation resulted in the isolation of 1,2,3,4,6-penta-O-galloyl-$\beta$-D-glucose (1) as an active principle responsible for the inhibition on $\alpha$-glucosidase, together with two related components 2 and 3. Compound 1 demonstrated a strong inhibition on the yeast $\alpha$-glucosidase, in vitro and $IC_{50}$ value was calculated as 0.96 mg/ml, when that of a reference drug, acarbose was estimated as 5.3 mg/ml. On the other hand, other related constituents of the species, 1,2,3,6-tetra-O-galloyl-$\beta$-D-glucose (2) and gallic acid (3) were exhibited relatively poor inhibition upon the yeast $\alpha$-glucosidase, respectively.

참두릅 잎의 Protein Tyrosine Phosphatase 1B와 α-Glucosidase 저해 활성 (Inhibitory Activity of Aralia elata Leaves on Protein Tyrosine Phosphatase 1B and α-Glucosidase)

  • 조윤숙;성수희;바크타 히만수 쿠마르;정희진;문경호;최재수
    • 생약학회지
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    • 제47권1호
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    • pp.29-37
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    • 2016
  • Anti-diabetic potential of the leaves of A. elata through the inhibitory activity on PTP1B and ${\alpha}$-glucosidase has not been reported. In this study, the EtOAc fraction of methanolic extract from the leaves of A. elata showed potent inhibitory activity against the PTP1B and ${\alpha}$-glucosidase with $IC_{50}$ value of $96.29{\pm}0.3$ and $264.71{\pm}14.87{\mu}g/mL$, respectively. Three known triterpenoids, oleanolic acid, oleanolic acid-28-O-${\beta}$-D-glucopyranoside and oleanolic acid-3-O-${\beta}$-D-glucopyranoside were isolated from the most active EtOAc fraction. We determined the chemical structure of these triterpenoids through comparisons of published nuclear magnetic resonance (NMR) spectroscopic data. Furthermore, we screened these triterpenoids for their ability to inhibit PTP1B and ${\alpha}$-glucosidase over a range of concentrations ($12.5-50{\mu}M$). All three terpenoids significantly inhibited PTP1B in a concentration dependent manner and oleanolic acid effectively inhibited ${\alpha}$-glucosidase. In addition, these compounds revealed potent inhibitory activity with negative binding energies toward PTP1B, showing high affinity and tight binding capacity in the molecular docking studies. Therefore, the results of the present study clearly demonstrate that A. elata leaves and its triterpenoid constituents might be beneficial in the prevention or treatment of diabetic disease.

Diazotized Chitin에 고정된 $\beta$-glucosidase의 생물반응기에서의 특성, 물질전달계수 및 효율인자에 관한 연구 (Characteristics, Mass Transfer Coefficient and Effectiveness Factor of $\beta$-glucosidase Immobilized on the Diazotized Chitin in Bioreactors)

  • 김종덕;이경희;서석수
    • 한국식품영양과학회지
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    • 제20권5호
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    • pp.494-502
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    • 1991
  • Diazotized chitin(CHITN) as supports of immobilized enzyme, which was obtained by alkaline hydrolysed chitin with NaN3 and HCI was employed to produce CHITN-Gase with glutaraldehyde as bifunctional reagent. Activities of CHITN-Gase were determined with reaction of p-nitro-pheol-$\beta$-D-glucopyranoside(PNG) in plug flow reactor as a reference of CHITA-Gase. Their optimum temperature, pH, Km and Vmax, mass transfer coefficient (h), effctiveness factor(η)were plotted with variation of flow rate and H/D. Mass transfer coefficient(h) of those enzymes increased because of their flux, as flow rates were increased and controlled by reaction rate. Effectiveness factor(η) of both enzymes were nearly 1.0.

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Agrobacterium tumefaciens 유래 인디칸 분해활성을 갖는 β-glucosidase의 분리와 특성분석 (Purification and Characterization of an Indican-hydrolyzing β-glucosidase from Agrobacterium tumefaciens)

  • 황창선;이진영;김근중
    • KSBB Journal
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    • 제27권6호
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    • pp.341-346
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    • 2012
  • Indican (indoxyl-${\beta}$-D-glucoside) is a colorless natural compound and can be used as a precursor for the production of indigo. This production step only require an enzyme, ${\beta}$-glucosidase, that readily screened from microbial resource by using selective media supplemented with indican as a sole carbon source. Agrobacterium tumefaciens was well grown in this media and thus presumed to produce a related enzyme. The corresponding gene, encoding a protein with a calculated molecular mass of 51 kDa, was cloned and overexpressed as MBP fusion proteins. The purified enzyme was determined to be a dimer and showed the maximum activity for indican at pH 7.0 and $40^{\circ}C$. The kinetic parameters for indican, Km and Vmax, were determined to be 1.4 mM and 373.8 ${\mu}M/min/mg$, respectively. The conversion yield of indican into indigo using this enzyme was about 1.7-1.8 folds higher than that of previously isolated enzyme from Sinorhizobium meliloti. Additionally, this enzyme was able to hydrolyze various ${\beta}$-1,4 glycoside substrates.

순수 섬유소에 대한 고농도 당화공정의 동력학적 모사 (Kinetic Modeling of the Enzymatic Hydrolysis of $\alpha$-Cellulose at High Sugar Concentration)

  • 오경근;정용섭홍석인
    • KSBB Journal
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    • 제11권2호
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    • pp.151-158
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    • 1996
  • 섬유소는 효소에 의한 가수분해에 의하여 유용한 화학물질이냐 연료 등으로 전환될 수 있다. 그러나 효소가 온도나 전단응력에 의해 쉽게 비활성화 되고 생성물인 당에 의한 억제 효과가 심각하기 때문에 효과적인 당화공정이 이루어지지 못하는 실정이다. 본 실험에서는 섬유소 가수분해에서의 두 효소, 즉 셀룰라아제 와 ${\beta}$-glucosidase의 통력학적 특정틀 을 이해하고, 생성물 억제영향 빛 효소의 비활성화 를 관찰하여, 섬유소의 고농도 당화 공정에 적용가 능한 통력학적 이론을 규명하고자 하였다. 셀룰라아제 벚 ${\beta}$-glucosidase는 다양한 통력학적 특정들을 보였으며, 반응기내에 5gN 의 포도당이 존재하여도 $\beta$glucosidase의 역가가 70% 이상 감소하는 것으로 나타나, 포도탕에 의한 ${\beta}$-glucosi­d dase의 억 제 영향이 가장 심각한 것으로 나타났다. 또한 셀로바이오스의 농도가 109/p 일때 역시 셀롤 라야제의 역가가 약 70% 감소하였다. ${\beta}$-glucosi dase의 경우 셀룰라아제와 비교하여 약 1.6배 정도 비활성화에 더 민강한 것으로 밝혀졌다. 당화 공정 모사 결과는 대체척으로 신뢰할 수 있는 범위의 결 과를 얻었으며, 가수분해가 진행되는동안 실험결과 와 모사에 의한 계산값은 잘 일치하였다.

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팔당호에서 종속영양 활성도의 계절적 변화 및 세균의 세포외 효소활성 (Seasonal Fluctuations of Heterotrophic Activity and Bacterial Extracellular Enzyme Activity in Paldang Lake)

  • 김상진
    • 미생물학회지
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    • 제31권1호
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    • pp.93-98
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    • 1993
  • 수계생태계에서 유기물질의 순환을 이해하기 위하여 팔당호에서 종속영양 활성도와 세균세포의 효소활성의 계절절 변화를 연구하였다. 팔당호 I 의 glucose 전환시간은 수층, 퇴적토에서 2-1,300 시간, 17-170 시간, protein hydrolysate 는 5-900 시간, 15-240 시간, acetic acid 는 4-350 시간, 15-230 시간으로 계절적인 변화를 나타냈다. Glucose, protein hydrolysate, acetate 각각의 호흡율은 수층에서 23-32%, 38-41%, 22-28%로 나타났고 퇴적토에서는 34%, 61% and 41% 로 나타났다. 이 결과로 3가지 유기물질 종류 모두가 수층보다 퇴적토에서는 높은 율로 호흡됨을 알 수 있었다. 한편 세균의 $\alpha$-glucosidase, $\beta$-glucosidase, N-acetyl-$\beta$-D-glucosaminidase, aminopeptidase 활성력을 살펴본 결과 수층에서는 효소 각각에 대해 32-44%, 31-32%, 18-34% 61-67% 의 범위를 나타내었고 퇴적토에서는 34%, 40%, 23% 65%로 나타났다.

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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.

Purification and Characterization of an Extracellular ${\beta}$-Glucosidase Produced by Phoma sp. KCTC11825BP Isolated from Rotten Mandarin Peel

  • Choi, Jung-Youn;Park, Ah-Reum;Kim, Yong-Jin;Kim, Jae-Jin;Cha, Chang-Jun;Yoon, Jeong-Jun
    • Journal of Microbiology and Biotechnology
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    • 제21권5호
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    • pp.503-508
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    • 2011
  • A ${\beta}$-glucosidase from Phoma sp. KCTC11825BP isolated from rotten mandarin peel was purified 8.5-fold with a specific activity of 84.5 U/mg protein. The purified enzyme had a molecular mass of 440 kDa with a subunit of 110 kDa. The partial amino acid sequence of the purified ${\beta}$-glucosidase evidenced high homology with the fungal ${\beta}$- glucosidases belonging to glycosyl hydrolase family 3. Its optimal activity was detected at pH 4.5 and $60^{\circ}C$, and the enzyme had a half-life of 53 h at $60^{\circ}C$. The $K_m$ values for p-nitrophenyl-${\beta}$-D-glucopyranoside and cellobiose were 0.3 mM and 3.2 mM, respectively. The enzyme was competitively inhibited by both glucose ($K_i$=1.7 mM) and glucono-${\delta}$-lactone ($K_i$=0.1 mM) when pNPG was used as the substrate. Its activity was inhibited by 41% by 10 mM $Cu^{2+}$ and stimulated by 20% by 10 mM $Mg^{2+}$.