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2 "Vibrio sp."
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Research Support, Non-U.S. Gov't
The Influence of NaCl and Carbonylcyanide-m-Chlorophenylhydrazone on the Production of Extracellular Proteases in a Marine Vibrio Strain
Young Jae Kim
J. Microbiol. 2004;42(2):156-159.
DOI: https://doi.org/2028 [pii]
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AbstractAbstract
In general, the salinity of the ocean is close to 3.5% and marine vibrios possess the respiratory chainlinked Na+ pump. The influence of sodium chloride and the proton conductor carbonylcyanide m-chlorophenylhydrazone (CCCP) on the production of extracellular proteases in a marine Vibrio strain was examined. At the concentration of 0.5 M, sodium chloride minimally inhibited the activity of extracellular proteases by approximately 16%, whereas at the same concentration, the producton of extracellular proteases was severely inhibited. On the other hand, the production of extracellular proteases was completely inhibited by the addition of 2 μM CCCP at pH 8.5, where the respiratory chain-linked Na^+ pump functions.
Purification and Characterization of Chitinase from a Marine Bacterium, Vibrio sp. 98CJ11027
Shin Hye Park , Jung-Hyun Lee , Hong Kum Lee
J. Microbiol. 2000;38(4):224-229.
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AbstractAbstract
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 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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