Journal of Microbiology and Biotechnology

  • 제10권1호
  • /
  • Pages.103-106
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  • 2000
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  • 1017-7825(pISSN)
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  • 1738-8872(eISSN)
한국미생물·생명공학회 (The Korean Society for Microbiology and Biotechnology)
권호 표지

Influence of Temperature, Oxygen, m-Chlorophenylhydrazone Cerulenin, and Quinacrine on the Production of Extracellular Proteases in Bacillus cereus

  • Kim, Sam-Sun (Department of Microbiology, College of Natural Sciences, Changwon National University, Department of Agricultural Chemistry, Kyungpook National University) ;
  • Park, Yong-Ha (Korea Research Institute of Bioscience and Biotechnology, KIST) ;
  • Rhee, In-Koo (Department of Agricultural Chemistry, Kyungpook National University) ;
  • Kim, Young-Jae (Department of Microbiology, College of Natural Sciences, Changwon National University)
  • 발행 : 2000.02.01
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초록

Bacillus cereus KCTC 3674 excretes at least two kinds of extracellular proteases into the growth medium. Two major bands of the protease activity with molecular weights of approximately 100 and 38 kDa were obtained after gelatin-SDS-PAGE. The protease with a molecular weight of 38kDa was identified as an extracellular neutral (metallo-) protease. The neutral protease was quite thermostabile but labile to alkaline pH. On the contrary, the 100-kDa protease was thermolabile but stable to alkaline pH. The production of 38-kDa neutral protease was strongly affected by temperature, oxygen, carbonylcyanied m-chlorophenylhydrazone(CCCP) that was defined as a protonophofre, and cerulenin which inhibited lipid synthesis and caused changes in the membrane composition. On the other hand, the production of the 100-kDa protease was strongly affected by only temperature and cerulenin. Quinacrine (0.2 mM), which inhibits the penicillinase-releasing proteases of Bacillus licheniformis, had no effect, whatsoever, on the production of extracellular proteases in B.cereus KCTC 3674.

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참고문헌

  1. Biochim. Biophys. Acta v.1264 Cloning and primary structure of a ne hemolysin gene from Bacillus cereus. Baida, G. E.;N. P. Kuzmin
  2. J. Bacteriol. v.138 Export of extracellular levansucrase by Bacillus subtilis: Inhibition by cerulenin and quinacrine. Caulfield, M. P.;R. C. W. Berkeley;E. A. Pepper;J. Melling
  3. Bergey's Mannual of Systematic Bacteriology v.2 Genus Bacillus cohn 1986 Claus, D.;R. C. W. Berkeley.;P. H. A. Sneath(ed)
  4. Clin. Microbiol. Rev. v.6 Bacillus cereus and related species. Drobniewski, F. A.
  5. J. Bacteriol. v.134 Evidence linking penicillinase formation and secretion to lipid metabolism in Bacillus licheniformis. Fishman, Y. S.;Rottem;N. Citri.
  6. J. Food Prot. v.47 Bacillus cereus foodborne illness -an update. Johnson, K. M.
  7. Biochemistry v.34 Rho-ADP-ribosylating exoenzyme from Bacillus cereus. Purification, characterization, and identification of the NAD-binding site. Just, I.;J. Selzer;M. Jung;J. van Damme;J. Vandekerckove;K. Aktories
  8. Biosci. Biotechnol. Biochem. v.63 cAMP mediated catabolite repression and electrochemical potential dependent production of an extracellular amylase in Vibrio alginolyticus. Kim, O. K.;K. Hahm;Y. Park;Y. J. Kim
  9. J. Microbiol. Biotechnol. v.8 Taxonomic studies of the beta hemolysis causing pathogen Bacillus cereus isolated from sea water. Kim, S. .S;Y. Park;J. Lee;J. Yoon;Y. Shin;I. Rhee;Y. J. Kim
  10. Foodborne Bacterial Pathogens. Bacillus cereus and other Bacillus species;M. P. Doyle(ed) Kramer, J. M.;R. J. Gilbert
  11. Nature v.227 Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Laemmli, U.K.
  12. Bacteriol. Rev. v.40 The antibiotic cerulenin, a novel tool for biochemistry as an inhibitor of fatty acid synthesis Omura, S.
  13. J. Gen. Microbiol. v.118 Cerulenin inhibits production of extracellular proteins but not membrane proteins in Bacillus amyloliquefaciens. Paton, J. C.;B. K. May;W. H. Elliott.
  14. Appl. Microbiol. Biotechnol. v.25 A neutral protease produced by Bacillus cereus with high sequence homology to thermolysin: Production. Isolation and characterization. Sidler, W. B.;Kumpf;B. Peterhans;H. Zuber
  15. J. Bacteriol. v.129 Vesicle penicillinase of Bacillus licheniformis: Existence of periplasmic-releasing factors. Traficante, L. J.;J. O. Lampen.
  16. Mol. Microbiol. v.6 The role of the pro-sequence in the processing and secretion of the thermolysin-like neutral protease from Bacillus cereus. Wetmore, D. R.;S. L. Wong;R. S. Roche.