742
Views
17
CrossRef citations to date
0
Altmetric
Original Articles

Purification, Characterization, and Gene Sequencing of a Catalase from an Alkali- and Halo-tolerant Bacterium, Halomonas sp. SK1

, , &
Pages 955-962 | Received 10 Oct 2001, Accepted 15 Jan 2002, Published online: 22 May 2014

  • 1) Nadler, V., Goldberg, I., and Hochman, A., Comparative study of bacterial catalases. Biochim. Biophys. Acta, 882, 234-241 (1986).
  • 2) Zamocky, M., and Koller, F., Understanding the structure and function of catalase: clues from molecular evolution and in vitro mutagenesis. Prog. Biophys. Mol. Biol., 72, 19-66 (1999).
  • 3) Kono, Y., and Fridovich, I., Isolation and characterization of the pseudocatalase of Lactobacillus plantarum.J. Biol. Chem., 258, 6015-6019 (1983).
  • 4) Allgood, G. S., and Perry, J. J., Characterization of a manganese-containing catalase from the obligate thermophile Thermoleophilum album.J. Bacteriol., 168, 563-567 (1986).
  • 5) Kagawa, M., Murakoshi, N., Nishigawa, Y., Matsumoto, G., Kurata, Y., Mizobata, T., Kawata, Y., and Nagai, J., Purification and cloning of a thermostable manganese catalase from a thermophilic bacterium. Arch. Biochem. Biophys., 362, 346-355 (1999).
  • 6) Whittaker, M. M., Barynin, V. V., Antonyuk, S. V., and Whittaker, J. W., The oxidized (3,3) state of manganese catalase. Comparison of enzymes from Thermus thermophilus and Lactobacillus plantarum.Biochemistry, 38, 9126-9136 (1999).
  • 7) Demirjian, D. C., Moris-Varas, F., and Cassidy, C. S., Enzymes from extremophiles. Curr. Opin. Chem. Biol., 2, 144-151 (2001).
  • 8) Niehaus, F., Bertoldo, C., Kahler, M., and Antranikian, G., Extremophiles as a source of novel enzymes for industrial application. Appl. Microbiol. Biotechnol., 6, 711-729 (1999).
  • 9) Vigo, T. L., Textile processing and properties: preparation, dyeing, finishing, and performance. Elsevier Science, USA, 11, 112-192 (1994).
  • 10) Loprasert, S., Negoro, S., and Okada, H., Thermostable peroxidase from Bacillus stearothermophilus.J. Gen. Microbiol., 134, 1971-1976 (1988).
  • 11) Brown-Peterson, N., and Salin, L., Purification and characterization of a mesohalic catalase from the halophilic bacterium Halobacterium halobium.J. Bacteriol., 177, 387-384 (1995).
  • 12) Yumoto, I., Fukumori, Y., and Yamanaka, T., Purification and characterization of catalase from a facultative alkalophilic Bacillus. J. Biochem., 108, 583-587 (1990).
  • 13) Yumoto, I., Ichihashi, D., Iwata, H., Istokovics, A., Ichise, N., Matsuyama, H., Okuyama, H., and Kawasaki, K., Purification and characterization of a catalase from the facultatively psychrophilic bacterium Vibrio rumoiensis S-1T exhibiting high catalase activity. J. Bacteriol., 182, 1903-1909 (2000).
  • 14) Weisburg, W. G., Barns, S. M., Pelletier, D. A., and Lane, D. J., 16S Ribosomal DNA amplification for phylogenic study. J. Bacteriol., 173, 2, 697-703 (1991).
  • 15) Altschul, S. F., Gish, W., Miller, W., Myers, E. W., and Lipman, D. J., Basic local alignment search tool. J. Mol. Biol., 215, 403-410 (1990).
  • 16) Thomson, J. D., Higgins, D. G., and Gibson, T. J., CLUSTAL W: improving the sensitivity of progressive multiple sequence weighing, position specific gap penalties and weight matrix choice. Nucleic Acids Res., 76, 4350-4354 (1994).
  • 17) Beers, R. F., and Sizer, I. W., A spectrophotometric method for measuring the breakdown of hydrogen peroxide by catalase. J. Biol. Chem., 195, 113 (1952).
  • 18) Bradford, M. M., A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem., 72, 248-254 (1976).
  • 19) Laemmli, U. K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 277, 680-685 (1970).
  • 20) Gregory, E. M., and Fridovich, I., Visualization of catalase on acrylamide gels. Anal. Biochem., 58, 57-62 (1974).
  • 21) Woodbury, W., Spencer, A. K., and Stahman, M. A., An improved procedure using ferricyanide for detecting catalase isozymes. Anal. Biochem., 44, 301-305 (1971).
  • 22) Murray, M. G., and Thompson, W. F., Rapid isolation of high molecular weight plant DNA. Nucleic Acids Res., 8, 4321-4325 (1980).
  • 23) Ichise, N., Morita, N., Hoshino, T., Kawasaki, K., Yumoto, I., and Okuyama, H., A mechanism of resistance to hydrogen peroxide in Vibrio rumoiensis S-1. Appl. Environ. Microbiol., 65, 73-79 (1999).
  • 24) Kuusk, H., Bjorklund, M., and Rydstrom, J., Purification and characterization of a novel bromoperoxidase-catalase isolated from bactetria found in recycled pulp white water. Enzyme Microb. Technol., 28, 617-624 (2001).
  • 25) Vreeland, R. H., Section 4. Gram-negative aerobic rods and cocci, Genus Halomonas Vreenad, Litchfield, Martin and Elliot 1980, 494VP. In “Bergey's Manual of Systematic Bacteriology”, vol. 1., eds. Krieg, N. R., and Holt, J. G., the Williams & Wilkins, Baltimore/London, pp. 340-343 (1984).
  • 26) Romano, I., Nicolaus, B., Lama, L., Manca, M. C., and Gambacorta, A., Characterization of a haloalkalophilic strictly aerobic bacterium, isolated from Pantelleria island. Syst. Appl. Microbiol., 19, 326-333 (1996).
  • 27) Pettigrew, G. W., and Brown, K. R., Free and membrane-bound forms of bacterial cytochrome c4. Biochem. J., 252, 427-435 (1988).
  • 28) Hough, D. W., and Danson, M. J., Extremozymes. Curr. Opin. Chem. Biol., 3, 39-46 (1999).
  • 29) Baumann, P., Furniss, A. L., and Lee, J. V., Section 5 Facultatively anaerobic Gram-negative rods, Genus I. Vibrio Pacini 1857, 411AL. In “Bergey's Manual of Systematic Bacteriology”, vol. 1., eds. Krieg, N. R., and Holt, J. G., the Williams & Wilkins, Baltimore/London, pp. 518-538 (1984).
  • 30) Van den Burg, B., Vriend, G., Veltman, O. R., Venema, G., Eijsink, V. G., Engineering an enzyme to resist boiling. Proc. Natl. Acad. Sci. U. S. A., 95, 2056-2060 (1998).

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.