• Title/Summary/Keyword: Anabaena cylindrica

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Characterization of the Bacterial Cell Wall Lytic Enzyme Produced by Aspergillus sp. HCLF-4 (Aspergillus sp. HCLF-4에 의해 생성되는 세균세포벽 분해효소의 특성)

  • 임진하;민병례;최영길
    • Korean Journal of Microbiology
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    • v.37 no.1
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    • pp.15-20
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    • 2001
  • In this study, we have isolated bacterial cell wall lytic enzyme in the culture supernatant of Aspergillus sp. HCLF-4. This hydrolase showed cell wall lytic activity against Anabaena cylindrica. The extracellular enzyme was produced by Aspergillus sp. HCLF-4 when it was grown in a PDB media containing 0.05% heat killed Micrococcus luteus cells. The molecular weight of lytic enzyme was about 14.3 kDa. The optimal pH and temperature for the activity of this enzyme were 3.0~4.0 and $30^{\circ}C$, respectively. This hydrolase activity was reduced by $Na^{+}$, $Li^{+}$, $Ca^{2+}$, $Cu^{2+}$, $Fe^{3+}$, EDTA, and PMSF, whereas it was increased by $Mg^{2+}$, $Mn^{2+}$>. The enzyme has N-acetylmuramyl-L-amidase or endopeptidase activity.

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Purification and Characterization of Extracellular $\beta$-Glucosidase from Sinorhizobium kostiense AFK-13 and Its Algal Lytic Effect on Anabaena flos-aquae

  • Kim, Jeong-Dong;Lee, Choul-Gyun
    • Journal of Microbiology and Biotechnology
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    • v.17 no.5
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    • pp.745-752
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    • 2007
  • A $\beta$-glucosidase from the algal lytic bacterium Sinorhizobium kostiense AFK-13, grown in complex media containing cellobiose, was purified to homogeneity by successive ammonium sulfate precipitation, and anion-exchange and gel-filtration chromatographies. The enzyme was shown to be a monomeric protein with an apparent molecular mass of 52 kDa and isoelectric point of approximately 5.4. It was optimally active at pH 6.0 and $40^{\circ}C$ and possessed a specific activity of 260.4 U/mg of protein against $4-nitrophenyl-\beta-D-glucopyranoside$(pNPG). A temperature-stability analysis demonstrated that the enzyme was unstable at $50^{\circ}C$ and above. The enzyme did not require divalent cations for activity, and its activity was significantly suppressed by $Hg^{+2}\;and\;Ag^+$, whereas sodium dodecyl sulfate(SDS) and Triton X-100 moderately inhibited the enzyme to under 70% of its initial activity. In an algal lytic activity analysis, the growth of cyanobacteria, such as Anabaena flos-aquae, A. cylindrica, A. macrospora, Oscillatoria sancta, and Microcystis aeruginosa, was strongly inhibited by a treatment of 20 ppm/disc or 30 ppm/disc concentration of the enzyme.

The study on the Fluorescence Characteristics of Several Freshwater Bloom Forming Algal Species and Its Application (수종 담수적조 원인종들의 형광특성과 적용연구)

  • Son, Moon-Ho;Zulfugarov, Ismayil S.;Kwon, O-Seob;Moon, Byoung-Young;Chung, Ik-Kyo;Lee, Choon-Hwan;Lee, Jin-Ae
    • ALGAE
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    • v.20 no.2
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    • pp.113-120
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    • 2005
  • The freshwater blooms mainly blue-green algal blooms occur frequently in the lower Naktong River in summer, which provoke many socio-economical problems; therefore, the early detection of bloom events are demanding through the quantitative and qualitative analyses of blue green algal species. The in vivo fluorescence properties of cultured strains of Microcystis aeruginosa, M. viridis, M. wesenbergii, M. ichthyoblabe, Anabaena cylindrica, A. flos-aquae, and Synedra sp. were investigated. Wild phytoplankton communities of the lower Naktong River were also monitored at four stations in terms of their standing stocks, biomass and fluorescence properties compared with its absorption spectram. The 77K fluorescence emission spectra of each cultured strains normalized at 620 nm was very specific and enabled to detect of blue green algal biomass qualitatively and quantitatively. The relative chlorophyll a concentration determined by chlorophyll fluorescence analysis method showed significant relationship with chlorophyll a concentration determined by solvent extraction method ($R^2$ = 0.906), and the blue-green algal cell number determined by microscopic observation ($R^2$ = 0.588), which gives insight into applications to early detection of blue green algal bloom.