Journal of Microbiology and Biotechnology

The Korean Society for Microbiology and Biotechnology (한국미생물·생명공학회)
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Purification and Characterization of Extracellular Chitinase Produced by Marine Bacterium, Bacillus sp. LJ-25

  • Lee, Jung-Suck (Graduate School of Agricultural Science, Tohoku University) ;
  • Joo, Dong-Sik (East Coastal Marine Bioresources Research Center, Kangnung National University) ;
  • Cho, Soon-Yeong (East Coastal Marine Bioresources Research Center, Kangnung National University) ;
  • Ha, Jin-Hwan (Department of Food Science and Technology, Cheju National University) ;
  • Lee, Eung-Ho (Department of Food Science and Technology, Pukyong National University)
  • Published : 2000.06.01
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Abstract

Abstract Extracellular chitinase was purified from the culture liquid of the marine bacterium, Bacillus sp. LJ-25 , and its enzymatic properties were examined. The purified chitinase exhibited a single band on SDS-PAGE and the molecular weight was estimated to be approximately 50 kDa. The optimum pH and temperature for the enzymatic activity were 7.0 and $35^{\circ}C$, respectively. The activity of the chitinase was strongly inhibited by $Zn^{2+}$ and slightly inhibited by $Ba^{2+},{\;}Co^{2+},{\;}Mn^{2+},{\;}and{\;}Cu^{2+}$. The purified chitinase did not hydrolyze $p-nitrophenolN-acetyl-{\bata}-D-glucosaminide{\;}(GlcNAc)_2$ and Micrococcus lysodeikticus cells, which are known to be the substrates for exo-type chitinase. Among the hydrolyzates of colloidal chitin, $(GlcNAc)_2$ was in the highest concentration with small amounts of GlcNAc and $(GlcNAc)_3$..

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