• Title/Summary/Keyword: Streptomyces sp. MET 0515

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Purification and characterization of the extracellular alginate lyase from Streptomyces sp. MET 0515 (Streptomces sp. MET 0515의 균체외 Alginate lyase의 정제 및 특성)

  • Kim, Hyun-Kyoung;Lee, Jae-Chang;Kang, Nam-Hyun;Kim, Song-Hee;Kim, Jong-Guk;Chung, Ki-Chul
    • Journal of Life Science
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    • v.17 no.5 s.85
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    • pp.625-633
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    • 2007
  • We isolated a new extracellular alginate lyase-producing microorganism, which displayed alginate-depolymerizing activity in plate assays, from coastal soils in Wando, Jeollanam-do, Korea. This alginate-depolymerizing bacterium belonged to the genus Streptomyces and it was named Streptomyces sp. MET 0515. An extracellular alginate lyase(ALY1) secreted by Streptomyces sp. MET 0515, was purified to homogeneity by a combination of acetone precipitation, anion-exchange chromatography (Q-Sepharose and DEAE-Sepharose) and Sephacryl S-200 HR gel filtration chromatography. Its molecular mass was 26 kDa as determined by SDS-PACE analysis. The enzyme had an optimal temperature of $70^{\circ}C$ for its activity, and was most active at pH 7.5. The thermal and pH stability were $0-50^{\circ}C$, and pH 6.0-9.0, respectively. The enzyme activity was stimulated by 1mM $Mn^{2+}$, and inhibited by 1mM $Fe^{3+}$, 1mM EDTA and 1mM $Zn^{2+}$. Preliminary analysis of substrate specificity showed that this alginate lyase had activity on both poly-alpha 1,4-L-guluronate and poly-beta 1,4-D-mannuronate in the alginate molecule.