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KMID : 0364819920300060501
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Korean Journal of Microbiology
1992 Volume.30 No. 6 p.501 ~ p.506
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Characterization of Extracellular Proteases from Alkalophilic Vibrio sp. Strain RH530
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Kwon, Yong Tae/권용태
Moon, Sun Young/Kim, Jin Oh/Kho, Yung Hee/Rho, Hyune Mo/문선염/김진오/고영희/노현모
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Abstract
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enrichment culture. The activity staining using gelatin SDS-polyacrylamide gel electrophoresis (PAGE) revealed that the strain produced an alkaline major protease (Apr B) with a size of 27 kDa, and at least six minor proteases. The apparent sizes of four of the minor proteases were approximately 45, 28, 22 and 19 kDa. Apr B and five of the minor proteases were inhibited by serine protease inhibitors including PMSF and DFP, suggesting that they are serine proteases. One of the minor proteases was inhibited by metalloprotease inhibitors, not by serine protease inhibitors, indicating it to be a metalloprotease. Furthermore, the activities of Apr B and Prt 3 were not inhibited by SDS in the reaction mixture. The production of Apr B and some of the minor proteases was specifically affected by culture temperature (30 to 37°C) and pH (7 to 10). The production of Apr B, Prt 2, Prt 5 and Prt 6 was mainly affected by culture temperature, while Prt 4 by culture pH. Prt 1 and Prt 3 were not affected by neither of these factors.
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KEYWORD
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Vibrio sp., gelatin SDS-PAGE, extracellular protease, proteases inhibitor, SDS-resistancy
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