Characterization of extracellular proteases from alkalophilic Vibrio sp. strain RH530 = 호 염기성 Vibrio sp. 균주 RH530의 세포외 단백질 분해효소의 특성
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- Characterization of extracellular proteases from alkalophilic Vibrio sp. strain RH530 = 호 염기성 Vibrio sp. 균주 RH530의 세포외 단백질 분해효소의 특성
- Yong-Tae Kwon; Sung-Young Moon; Jin-Oh Kim; Yung Hee Kho; Hyune-Mo Rho
- Bibliographic Citation
- Korean Journal of Microbiology, vol. 30, no. 6, pp. 501-506
- Publication Year
- An alkalophilic Vibrio sp. RH530 showing high proteolytic activity was isolated form soil samples by 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.deg.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.
- Vibrio sp.gelatin SDS-PAGEextracellular proteaseprotease inhibitorSDS-resistancy
- Korea Soc-Assoc-Inst
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- 1. Journal Articles > Journal Articles
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