• Title/Summary/Keyword: Streptomyces sp. M-20

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Inhibitory Effect of Metabolites isolated from Streptococcus mutas sp. M-20 on Glucosyltransferase Activity from Streptococcus mutans (Streptomyces sp. M-20 균의 대사물에 의한 Streptococcus mutans의 Glucosyltransferase 활성 억제 효과)

  • Kim, Kyoung-Ja
    • YAKHAK HOEJI
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    • v.49 no.2
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    • pp.122-127
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    • 2005
  • Dental caries is one of the most common oral diseases in the world. Glucosyltransferase (Gtase) of Streptococcus mutans (S. mutans) plays an important role in the develo pment of dental caries. For the purpose to develop anti- caries, we examined the effect of metabolites isolated from Streptomyces sp. M-20 on Gtase and the growth of S. mutans. Streptomyces sp. M-20 isolated from Mongolian soil showed 95~96% sequence homology with that of Streptomyces lin- colnensis. The metabolites of Streptomyces sp. M-20 were partially purified by extraction with ethyl acetate, silica gel column chromatography and preparative TLC. Partially purified metabolite, red colored component (MR-20) in ethyl acetate fraction showed potent antibacterial activitiy against S. mutans and inhibitory activity against Gtase purified from S. mutans, while another isolated yellow component (MY-20) showed no activity against S. mutans. The inhibitory activity of MR-20 against Gtase was confirmed by activity staining on SDS-polyacrylamide gel electrophoresis. The concentration of MR-20 for 50% inhibition $(IC_{50})$ against Gtase activity was $60{\mu}g/ml$. These results suggest that MR-20 can be developed for antibacterial agent and anticaries.

Selection of Beneficial Microbial Agents for Control of Fungal Diseases in the Phyllosphere of Cucumber Plant (오이 지상부의 주요 곰팡이 병해의 생물적 방제용 유용미생물의 선발)

  • Lee, Sang-Yeob;Lee, Young-Kee;Park, Kyung-Seok;Kim, Yong-Ki
    • The Korean Journal of Pesticide Science
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    • v.14 no.4
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    • pp.326-331
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    • 2010
  • Bacillus subtilis B29, B. subtilis M10 and Streptomyces sp. CC19 obtained from phyllosphere of cucumber plants were selected for biological control of fungal air-borne diseases. For the downy mildew, diseased area of B. subtilis B29, B. subtilis M10 and Streptomyces sp. CC19 showed 0.5%, 20.2% and 42.0%, but that of control was 82.0% respectively, in cucumber seedling test. Incidence of powdery mildew by once application of B. subtilis B29, B. subtilis M10 and Streptomyces sp. CC19 was 2.8%, 3.6% and 12.3%, respectively, whereas that of control was 65.6%. On the gray mold, diseased area of B. subtilis B29, B. subtilis M10 and Streptomyces sp. CC19 was 8.0%, 30.8% and 5.2%, respectively, compared to 81.2% for the control. Therefore, B. subtilis B29 could be a prospective antagonist for biological control of powdery mildew, downy mildew and gray mold of cucumber plant.

Properties of Chitobiase Produced by Streptomyces sp. (Strepsomyces속 균주가 생산한 Ghitobiase의 효소학적 성질)

  • 김중배
    • The Korean Journal of Food And Nutrition
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    • v.5 no.2
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    • pp.132-136
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    • 1992
  • Streptomyces sp. YB-88-20 was Isolated from soil and the properties of chitobiase were investigated. The optimal reaction condition for the enzyme was pH 5.5 and 4$0^{\circ}C$ , and was stable in the range of pH 4. 0 to 5.5 and temperature at 4$0^{\circ}C$, and 40 min, respectively The enzyme was inactivated by heating at 45$^{\circ}C$ for 1 hr. The enzyme was slightly activated by Mna+. Mg2+, but inhibited by Fea+. Km and activation energy was 1.5072 M and 8.314 kcal/mol.

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Characterization of Recombinant PolyG-Specific Lyase from a Marine Bacterium, Streptomyces sp. M3 (해양세균 Streptomyces sp. M3로 부터 얻은 재조합 polyG-specific lyase의 특성)

  • Kim, Hee-Sook
    • Journal of Life Science
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    • v.20 no.11
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    • pp.1582-1588
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    • 2010
  • A new alginate lyase gene of marine bacterium Streptomyces sp. M3 had been previously cloned in pColdI vector and transformed into E. coli BL21 (DE3). In this study, M3 lyase protein without signal peptide was overexpressed by induction with IPTG and purified with Ni-Sepharose affinity chromatography. The absorbance at 235 nm of the reaction mixture and TLC analysis showed that M3 alginate lyase was a polyG-specific lyase. When M3 lyase was assayed with substrate for 10 min, optimum pH and optimum temperature were pH 9 and $60^{\circ}C$. For the effect of 1mM metal ion on M3 lyase activity, $Ca^{++}$ and $Mn^{++}$ ions increased the alginate degrading activity by two-fold, whereas $Hg^{++}$ and $Zn^{++}$ ions inhibited the lyase activity completely. $Mg^{++}$, $Co^{++}$, $Na^+$, $K^+$, and $Ba^{++}$ did not show any strong effects on alginate lyase activity.

The Optimal Conditions for Fibrinolytic Enzyme Production from Streptomyces sp. JK-20 (Streptomyces sp. JK-20유래 혈전용해효소의 생산조건)

  • 정영기;전홍기;김유정
    • Journal of Life Science
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    • v.12 no.1
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    • pp.43-48
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    • 2002
  • An actinomycetes which produces fibrinolytic enzyme was isolated from soil. Characteristics of the isolated strain and the optimal conditions for the productions of fibrinolytic enzyme were summarized as follows; The fibrinolytic enzyme production strain generates gray airmycelium and had about 0.6~0.8$\times$0.4~0.8${\mu}{\textrm}{m}$ cylindrical spore, smooth surface and formed spore chain of 10~40 spores. We have identified this strain as Streptomyces sp. JK-20. This strain was able to grow up at 20~32$^{\circ}C$ and its optimum growth temperature and pH was 24$^{\circ}C$ and pH 6.0, respectively. The optimal conditions for porducing fibrinolytic enzyme; carbon source, nitrogen source, metal ions and phosphorous sources was 1% xylose, 0.5% yeast extract, 0.5% polypepton, 0.1% MgSO$_4$.7$H_2O$ and 0.1% NaH$_2$PO$_4$.2$H_2O$, respectively. This strain showed the highest productivity of fibrinolytic enzyme after the fourth day under such optimal culture conditions.

Purification and Characterization of Chitinase from Streptomyces sp. M-20

  • Kim, Kyoung-Ja;Yang, Yong-Joon;Kim, Jong-Gi
    • BMB Reports
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    • v.36 no.2
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    • pp.185-189
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    • 2003
  • Chitinase (EC 3.2.1.14) was isolated from the culture filtrate of Streptomyces sp. M-20 and purified by ammonium sulfate precipitation, DEAE-cellulose ion-exchange chromatography, and Sephadex G-100 gel filtration. No exochitinase activity was found in the culture filtrate. The molecular mass of the purified chitinase was 20 kDa, estimated by a sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and was confirmed by activity staining with Calcofluor White M2R. Chitinase was optimally active at pH of 5.0 and at $30^{\circ}C$. The enzyme was stable from pH 4 to 8, and up to $40^{\circ}C$. Among the metals and inhibitors that were tested, the $Hg^+$, $Hg^{2+}$, and p-chloromercuribenzoic acid completely inhibited the enzyme activity. The chitinase activity was high on colloidal chitin, chitotriose, and chitooligosaccharide. The purified chitinase showed antifungal activity against Botrytis cinerea, and lysozyme activity against the cell wall of Botrytis cinerea.

Valistatin (3-Amino-2-Hydroxy-4-Phenylbutanoyl-Valyl-Valine), a New Aminopeptidase M Inhibitor, Produced by Streptomyces sp. SL20209

  • Kho, Ying-Hee;Ko, Hack-Ryong;Chun, Hyo-Kon;Jung, Myung-Chul
    • Journal of Microbiology and Biotechnology
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    • v.5 no.1
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    • pp.36-40
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    • 1995
  • Valistatin, a new inhibitor of aminopeptidase M(AP-M) was discovered in the culture broth of Streptomyces sp. SL20209 isolated from a soil sample. The inhibitor was purified by extraction with n-butanol and the various column chromatographies, and then isolated as whitish powder. The $^1 H-and ^1 H, ^1 H-COSY$ NMR studies, amino acid analysis, and fragmentation patterns by FAB-MS suggested the presence of one 3-amino-2-hydroxy-4-phenylbutanoic acid and two valine residues in the inhibitor. Thus, the structure of valistatin was determined as 3-amino-2-hydroxy-4-phenylbutanoyl-valyl-valine. Valistatin has the molecular formular $C_20H_31N_3 O_5$ (MW 394), and its $IC_50$ value against hog kidney AP-M was determined to be 3.12 $mu g/ml$.

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An FMN-containing NADH-quinone reductase from streptomyces sp (An FMN-Containing NADH-Quinone Reductase from Streptomyces sp.)

  • Youn, Hong-Duk;Lee, Jin-Won;Youn, Hwan;Lee, Jeong-Kug;Hah, Yung-Chil;Kang, Sa-Ouk
    • Journal of Microbiology
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    • v.34 no.2
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    • pp.206-213
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    • 1996
  • NADH-quinone reductase was purified 22-fold from the cytosolic fraction of Streptomyces sp. Imsnu-1 to apparent hemogenity, with an overall yield of 9%, by the purification procedure consisting of ammonium, sulfate precipitation and DEAE Sephacryl S-200 and DEAE 5 PW chromatographies. Thes molecular mass of the enzyme determined by gel filtration chromatography was found to be 110 kDa. SDS-PAGE revealed that the enzyme consists of two sugunits with a molecular mass of 54 kDa. The enzyme contained 1 mol of FMN per subunit as a cofactor. The $A_{272}$ A$_{457}$ ratio was 6.14 and the molar extinction coefficients were calculated to be 20, 800 and 25, 400M$^{-1}$ $cm^{-1}$ / AT 349 AND 457 nm, respectively. The N-terminal sequence of the enzyme contained the highly conserved fingerprint of ADP-binding domain. The enzyme used NADH as an electron donor and various quinones as electron acceptors. Cytochrome c was practically inactive. Air-stable flavin semiquinone was produced by the addition of NADH to the enzyme. Also, naphthosemiquinone was detected in the reaction mixture containing the enzyme.

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Streptomyces sp. 50634 균주가 생산하는 tipA Promotor 활성화 물질, Sulfomycin Ia

  • Shim, Yong-Ho;Yun, Bong-Sik;Seto, Haruo;Hwang, Se-Young;Yoo, Ick-Dong
    • Microbiology and Biotechnology Letters
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    • v.25 no.6
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    • pp.586-591
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    • 1997
  • In the course of screening for the tipA promoter-inducing substances, we isolated an active compound, sulfomycin Ia, from the mycelium of a microorganism designated 50634. The producing organism was identified as Streptomyces sp. on the basis of taxonomic studies. Sulfomycin Ia was purified from mycelial extract by silica gel column chromatography, LH-20 column chromatography, silica gel TLC, and preparative HPLC. The molecular weight of sulfomycin Ia was determined to be m/z 1129 (M+Na)$^{+}$ by FAB mass measurement and $^{1}$H NMR spectroscopic analysis. The structure was assigned as a derivative of sulfomycin I with thiazole, methyloxazole, oxazole, and pyridine rings by $^{1}$H NMR spectral data.

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Purification and Characterization of Endoinulase from Streptomyces sp. S56 (Streptomyces sp. S56이 생산하는 Endoinulase의 정제 및 특성)

  • 김수일;하영주
    • Microbiology and Biotechnology Letters
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    • v.20 no.5
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    • pp.551-558
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    • 1992
  • The extracellular endoinulase from Streptomyces sp. 556 was purified and characterized, The culture broth was fractionated by ammonium sulfate saturation followed by DEAE-cellulose column chromatography and 5ephadex G-200 gel filtration, The ultimately purified fraction revealed a single band in 7.5% polyacrylamide gel electropherogram. The purified enzyme showed the maximal activity at pH 5.5-6.0 and $50^{\circ}C$, but lost 93% of inulase activity after 30 min incubation at $55^{\circ}C$ . The essen.tial amino acid residue for catalytic activity appeared to be tryptophan. This endo inulase was activated by $Mn^{2+}$, whereas inactivated by $Ag^{+}$, $Hg^{+}$, $Cu^{2+}$, $Zn^{2+}$, $Fe^{3+}$ and $Mo^{6+}$ EDTA and 8-hydroxyquinoline inhibited the enzyme so that the enzyme was considered to be a metalloenzyme. The Km value for inulin was 0.287 mM, and no invertase or $\alpha$-glucosidase activity was found in the enzyme.

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