• 제목/요약/키워드: Glycosidases

검색결과 42건 처리시간 0.029초

One-Step Enzymatic Synthesis of Blue Pigments from Geniposide for Fabric Dyeing

  • Cho, Y.J.;Kim, S.Y.;Kim, J.;Choe, E.K.;Kim, S.I.;Shin, H.J.
    • Biotechnology and Bioprocess Engineering:BBE
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    • 제11권3호
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    • pp.230-234
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    • 2006
  • In this study, we describe a one-step chemoenzymatic reaction for the production of natural blue pigments, in which the geniposide from Gardenia extracts is transformed by glycosidases to genipin. Genipin is then allowed to react with amino acids, thereby generating a natural blue pigment. The ${\beta}-glycosidases$, most notably Isolase (a variant of ${\beta}-glucanase$), recombinant ${\beta}-glycosidases$, Cellulase T, and amylases, were shown to hydrolyze geniposide to produce the desired pigments, whereas the ${\alpha}-glycosidases$ did not. Among the 20 tested amino acids, glycine and tyrosine were associated with the highest dye production yields. The optimal molar ratio of geniposide to glycine, two reactants relevant to pigment production, was unity The natural blue pigments produced in this study were used to dye cotton, silk, and wool. The color yields of the pigments were determined to be significantly higher than those of other natural dyes. Furthermore, the color fastness properties of these dyes were fairly good, even in the absence of mordant.

Changes of Glycosidase Activity of Frozen-Thawed Spermatozoa in Human

  • Lee, Chae-Sik;Lee, Sang-Chan;Lee, Ji-Eun;Cheong, Hee-Tae;Yang, Boo-Keun;Park, Choon-Keun
    • Reproductive and Developmental Biology
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    • 제35권2호
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    • pp.185-190
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    • 2011
  • To evaluate the effect of spermatozoa culture on glycosidase activity of frozen-thawed spermatozoa in human, the spermatozoa were treated experimentally and assayed for activities of ${\alpha}$-L-fucosidase, ${\alpha}$-D-mannosidase, ${\beta}$-D-galactosidase and N-acetyl-${\beta}$-D-glucosaminidase (${\beta}$-GlcNAc'ase). The ${\beta}$-GlcNAc'ase activity was at least two-folds higher than other glycosidases regardless of spermatozoa incubation (p<0.05). The spermatozoa motility was decreased with incubation periods, but no effects by different glycosidases on the changes of spermatozoa motility during the various periods of incubation. In all glycosidases, the spermatozoa-zona binding rates in spermatozoa without incubation were higher than in spermatozoa incubated for 2 h (p<0.05). ${\beta}$-GlcNAc'ase is present mainly in the plasma membrane of spermatozoa frozen-thawed in human. It was also shown that the glycosidase activity was increased in all glycosidases in spite of lower sperm-zona binding by spermatozoa incubation.

플라보노이드배당체에 의한 Bacteroides JY-6의 ${\beta}$-글루코시다제 및 ${\alpha}$-람노시다제의 유도 (Induction of ${\beta}$-Glucosidase and ${\alpha}$-Rhammosidase of Bacteroides JY-6 by Flavonoid Glycosides)

  • 장일성;박종백;김동현
    • 약학회지
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    • 제40권3호
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    • pp.335-339
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    • 1996
  • Optimal medium for growth and glycosidases production of Bacteroides JY-6, an human intestinal bacterium, was general anaerobic medium or tryptic soy broth containing sod ium thioglycolate and ascorbic acid. By cocultivation of Staphylococcus R-48, Bacteroides JY-6 could be cultured in LB broth unable to culture JY-6. Heated Staphylococcus R-48 was also the inducer of the production of Bacteroides JY-6 glycosidases. These glycosidases were induced well by natural flavonoid glycosides, such as poncirin, naringin and rutin, but were not by synthetic substrates, p-nitrophenyl ${\beta$-D-glucopyranoside and p-nitrophenyl ${\alpha}$-L-rhanmopyranoside.

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돼지 동결정액의 배양에 따른 체외수정능력과 Glycosidase Activity의 변화 (Changes of Glycosidase Activity and Fertilizing Ability in Vitro by Incubation of Frozen-Thawed Spermatozoa in the Pig)

  • 황인선;정희태;양부근;김정익;박춘근
    • 한국가축번식학회지
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    • 제27권2호
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    • pp.153-161
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    • 2003
  • 본 연구는 돼지 동결-융해 정자의 배양에 의한 체외수정능력과 glycosidase activity를 평가하기 위하여 chlortetracycfine fluorescence분석법을 이용하여, glycosidase가 체외수정능력과 정자침입에 미치는 영향에 대하여 검토하였다. 또한 돼지난자의 투명대내에서 발견된 당잔기에 대한 정자의 glyco-sidase 특이성을 확인하기 위하여 $\alpha$-L-fucosidase, $\alpha$-D-mannosidase, $\beta$-D-galactosidase 및 N-acetyl-$\beta$-D-glucosaminidase ($\beta$-GlcNAc'ase)의 activity를 분석하였다. 그 결과 glycosidase activity는 동결정자의 응해 후 배양하지 않았을 때보다 2시간 배양했을 때 더 높게 나타났다. $\beta$-GlcNAc'ase의 activity 는 정자 배양 유무에 관계없이 다른 glycosidase 처리시보다 최소한 2배 이상 높게 나타났다. 또한 첨체반응이 유기된 정자의 비율은 glycosidase ($\alpha$-D-mannosidase; P<0.05)에 의해 영향을 받았으며 자를 배양하지 않은 경우보다는 배양된 정자에서 높게 나타났다. 그러나 배양시간에 따른 정자의 존성에 대해 glycosidase의 종류에 따른 유의차는 인정되지 않았다. 한편 투명대내 정자의 접착과 입에 대한 또 다른 실험에서, 서로 다른 glyco-sidase가 첨가된 배양액내에서 수정된 정자가 배양시간이 길어짐에 따라 정자의 침입율은 낮아졌다 $\beta$-GlcNAc'ase; P<0.05). 투명대내의 정자접착정도는 glycosidase의 첨가시에 무첨가시보다 접착정도가 더 높았으며, 가장 높은 접착율은 $\beta$-GlcNAc'ase 첨가시 나타났다. 또한 모든 glycosidase 처리시 2시간 배양한 정자보다는 배양하지 않은 정자에서 투명대에 대한 접착정도가 높게 나타났으며, $\alpha$-D-mannosidase의 처리시 유의적인 차이를 보였다 (P<0.05). 본 연구의 결과, $\beta$-GlcNAc'ase가 주로 돼지정자의 원형질막내에 존재하는 것으로 추측되며, 배양된 정자에 의한 투명대 접착정도와 침입율이 낮았음에도 불구하고 glycosidase activity가 증가하는 것으로 나타났다.

Purification and Characterization of an α-D-Galactosidase from Grape Berry

  • Kang, Han-Chul;Kim, Tae-Su
    • Journal of Applied Biological Chemistry
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    • 제43권3호
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    • pp.141-146
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    • 2000
  • Glycosidase activities were tested from the grape berries, Vitis labruscana B. Takasumi. Among various glycosidases, $\alpha$-D-galactosidase was found to be the most active in the flesh and other glycosidases were considerably active in the order of the following: $\alpha$-D-mannosidase>$\alpha$-D-glucosidase>$\beta$-D-glucosidase>$\beta$-D-galactosidase. In the seeds, $\alpha$-D-glucosidase activity was the highest and other glycosidases such as $\alpha$-D-galactosidase, $\beta$-D-glucosidase, and $\beta$-D-galactosidase were still significantly active. The $\alpha$-D-galactosidase in the grape flesh was purified over 83-folds through salting-out with $(NH_4)_2SO_4$ and a series of chromatographies employing Sephadex G-50, Octyl-Sepharose, Q-Sepha- rose, and Biogel P-100. The enzyme was a monomer of 45 kDs as determined through SDS-PAGE and Sephacryl S-200 chromatography. The purified enzyme showed a preference of $\alpha$-D-galactose to $\beta$-D-galactose as a substrate about 5.4 times. Sulfhydryl specific reagents such as N-ethylmaleimide and iodoacetamide significantly inhibited the enzyme activity to the extents of 48 and 52% of its initial activity, respectively. The optimumpH range of $\alpha$-D-galactosidase was around 6.5-7.0. The enzyme activity increased by 46% in the presence of 1mM $Fe^{2+}$.

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Synthesis and Activity of a Potent ${\alpha}$-glucosidase inhibitor, (1R, 6R, 8S)-cis-1,6-dihydroxypyrrolizidine, and its isomer

  • Jung, Kyeong-Eun;Kang, Yong-Koo;Kim, Dong-Jin;Park, Sang-Woo
    • 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.

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잠뇨로부터 질소함유 당물질 분리 및 glycosidase에 대한 저해활성 (Isolation of N-Containing Sugars from Silkworm Urine and Their Glycosidase Inhibitory Activities)

  • 송주경;정성현
    • Biomolecules & Therapeutics
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    • 제6권4호
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    • pp.364-370
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    • 1998
  • Glycosidase inhibitors from urine of Bombyx mori were isolated and their inhibitory activities on glycosidases were evaluated. Six compounds were isolated by using several ion exchange columns, and their chemical structures were identified by the physicochemical and spectral data. Compound IV, V and Ⅵ were identified as 1-deoxynojirimycin, fagomine and 1,4-dideoxy-1,4-imino-D-arabinitol, respectively. Among six compounds isolated,1-deoxynojirimycin(IV) was the most potent inhibitor on $\alpha$-glucosidase and $\beta$-galactosidase of rat intestine, and its inhibitory activities for trehalase and almond $\beta$-glucosidase were relatively weak. Compound V and Ⅵl retained a little inhibitory potency toward $\alpha$-glucosidase and $\beta$-galactosidase. Compound II and III, however, have been found to have no effect on all glycosidases tested in this study.

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Complete Biotransformation of Protopanaxatriol-Type Ginsenosides in Panax ginseng Leaf Extract to Aglycon Protopanaxatriol by β-Glycosidases from Dictyoglomus turgidum and Pyrococcus furiosus

  • Yang, Eun-Joo;Shin, Kyung-Chul;Lee, Dae Young;Oh, Deok-Kun
    • Journal of Microbiology and Biotechnology
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    • 제28권2호
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    • pp.255-261
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    • 2018
  • Aglycon protopanaxatriol (APPT) has valuable pharmacological effects such as memory enhancement and tumor inhibition. ${\beta}$-Glycosidase from the hyperthermophilic bacterium Dictyoglomus turgidum (DT-bgl) hydrolyzes the glucose residues linked to APPT, but not other glycoside residues. ${\beta}$-Glycosidase from the hyperthermophilic bacterium Pyrococcus furiosus (PF-bgl) hydrolyzes the outer sugar at C-6 but not the inner glucose at C-6 or the glucose at C-20. Thus, the combined use of DT-bgl and PF-bgl is expected to increase the biotransformation of PPT-type ginsenosides to APPT. We optimized the ratio of PF-bgl to DT-bgl, the concentrations of substrate and enzyme, and the reaction time to increase the biotransformation of ginsenoside Re and PPT-type ginsenosides in Panax ginseng leaf extract to APPT. DT-bgl combined with PF-bgl converted 1.0 mg/ml PPT-type ginsenosides in ginseng leaf extract to 0.58 mg/ml APPT without other ginsenosides, with a molar conversion of 100%. We achieved the complete biotransformation of ginsenoside Re and PPT-type ginsenosides in ginseng leaf extract to APPT by the combined use of two ${\beta}$-glycosidases, suggesting that discarded ginseng leaves can be used as a source of the valuable ginsenoside APPT. To the best of our knowledge, this is the first quantitative production of APPT using ginsenoside Re, and we report the highest concentration and productivity of APPT from ginseng extract to date.

Testosterone과 dibutyryl cyclic AMP가 거세한 흰쥐 부정소의 $\beta$ -glucosidase와 몇가지 glycosidase 활성에 미치는 영향 및 부정소 상피세포의 여러 유형에 관한 연구 (Studies on Adivitie of $\beta$-Glucuronidase and Several Glycosidases of the Castrated Rat Epi-didymis Treated with Testosterone and Dibutyryl cAMP and the Cell Types of Epididymal Epithelium)

  • 최임순;정경순
    • 한국동물학회지
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    • 제32권3호
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    • pp.290-303
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    • 1989
  • $\beta$-glucosidase, $\beta$-glucuronidase, N-acetyl-$\beta$-glucosaminidase의 성적 성숙과의 연관서을 조사하기 위하여 흰쥐의 복강내로 testosterone과 dibutryjry cyclic AMP 를 투여하여 위이 효소들의 활성도를 측정하였다. 그 결과 겨세한 실험군에서$\beta$-glucosidase와 N-acetyl-$\beta$-glucosaminidase이 활성도도 거세후 7일째에는 유의성있는 감소효과를 나타내었다. testosterone을 7일간 계속 투여한 경우에는 세 효소의 활성도가 모두 유의성있게 증가하였고 dbcAMP 투여군의 경우는 거세 14일째되는 실험군과 비슷하거나 감소하는 경향이 있었다. 미세구조를 관찰한 결과 부정소 상피세포의 유형은 크게 주세포와 기저세포로 나눌 수 있었으며 주세포는 일반적인 원주상피의 형태를 나타냈으며 소낭을 많이 포함하고 있는 narrow cell이 존재하였다. 특히 부정소미에는 다른 상피세포에 비해 전자밀도가 낮은 light cell이 존재했고 기저세포는 부정소 부위마다 비슷한 형태를 가지는 것으로 나타났으며 상피세포 사이에는 이동능력을 가진 halo cell이 존재했다.

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인삼 Saponin이 Lysosome 효소 활성에 미치는 영향 (Effects of Ginseng Saponin on the Lysosomal Enzyme Activities in Streptozotocin-induced Diabetic Mice)

  • 문창규;김희수;김강석
    • 한국식품위생안전성학회지
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    • 제9권3호
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    • pp.105-109
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    • 1994
  • Lysosomal enzymes might play a most important role in the pathogenesis od diabetic microangiopathy. Some glycosidases, which participate in the catabolism of glycoprotein, are significantly decreased in diabetic mice. In search of new potential lysosomal enzyme inducers, we examined the effects of crude red-ginseng saponin fraction on N-acetyl-$\beta$-D-glucosaminidase, $\beta$-D-galactosidase and $\alpha$-D-mannosidase activities in the liver and kidney of normal and streptozotocin induced diabetic mice. It was found that i.p. administration of ginseng saponin produced the induction of lysosomal enzymes in the kidney more intensively than in the liver. The obtained results suggest the possibility that ginseng saponin might prevent the diabetic microangiopathy.

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