Purification and Characterization of Chitinase from a Marine Bacterium, Vibrio sp. 98CJ11027

  • Park, Shin-Hye (Microbiology Laboratory, Korea Ocean Research & Development Institute) ;
  • Lee, Jung-Hyun (Microbiology Laboratory, Korea Ocean Research & Development Institute) ;
  • Lee, Hong-Kum (Microbiology Laboratory, Korea Ocean Research & Development Institute)
  • Published : 2000.12.01

Abstract

Chitin-degrading marine bacterial strain 98CJ11027 was isolated from bryozoa from the coastal area of Cheju Island, Korea, and identified as a member of the genus Vibrio. The molecular mass of the main extracellular chitinase (chitinase I), purified from strain 98CJ11027, was estimated to be 98 kDa. The optimal condition for chitinase I activity is pH 6.0 and 45$^{\circ}C$. The activity was inhibited by Fe$\^$+2/ and Cu$\^$+2/. Chitinase I displayed the hydrolysis type of chitobiosidase and catalyzed reversed hydrolysis leading to the synthesis of tetraacetylchitotetraose.

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