Characterization of a facultatively psychrophilic bacterium, Vibrio rumoiensis sp. nov., that exhibits high catalase activity

Applied and Environmental Microbiology

Volumn 65, Issue 1, 1999, Pages 67-72

  Yumoto, Isao ^a   Iwata, Hideaki ^a,b   Sawabe, Tomoo ^c   Ueno, Keisuke ^a   Ichise, Nobutoshi ^a,c   Matsuyama, Hidetoshi ^b   Okuyama, Hidetoshi ^a,c   Kawasaki, Kosei ^a  

^a NATIONAL INSTITUTE OF ADVANCED INDUSTRIAL SCIENCE AND TECHNOLOGY AIST   (Japan)

^b TOKAI UNIVERSITY   (Japan)

^c HOKKAIDO UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

CELLS; DNA; ELECTRON MICROSCOPY; ELECTROPHORESIS; ENZYMES; FOOD PRODUCTS PLANTS; GELS; GENES; HYDROGEN PEROXIDE; MICROBIOLOGY; RNA; TEMPERATURE;

BLEBS; CATALASE ACTIVITY; CORYNEBACTERIUM GLUTAMICUM; FACULTATIVELY PSYCHROPHILIC BACTERIUM; FISH PRODUCT PROCESSING PLANT; POLYACRYLAMIDE GEL ELECTROPHORESIS; PSEUDOMONAS FLUORESCENS; STAPHYLOCOCCUS AURENS; TAXONOMIC POSITION; VIBRIO RUMOIENSIS;

BACTERIA;

BACTERIAL ENZYME; CATALASE; HYDROGEN PEROXIDE; RNA 16S;

ARTICLE; BLEACHING; CONTROLLED STUDY; CORYNEBACTERIUM GLUTAMICUM; DNA DNA HYBRIDIZATION; ELECTRON MICROSCOPY; ENZYME ACTIVITY; FOOD INDUSTRY; NONHUMAN; NUCLEOTIDE SEQUENCE; PHENOTYPE; POLYACRYLAMIDE GEL ELECTROPHORESIS; PSEUDOMONAS FLUORESCENS; RNA SEQUENCE; STAPHYLOCOCCUS AUREUS; TAXONOMY; TEMPERATURE; VIBRIO; VIBRIO RUMOIENSIS;

BACTERIA (MICROORGANISMS); BOVINAE; CORYNEBACTERIUM GLUTAMICUM; NEGIBACTERIA; PSEUDOMONAS; PSEUDOMONAS FLUORESCENS; STAPHYLOCOCCUS; STAPHYLOCOCCUS AUREUS; VIBRIO; VIBRIO RUMOIENSIS;

EID: 0032931848     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/aem.65.1.67-72.1999     Document Type: Article

References (33)

1. Antranikian, G., C. Herzberg, F. Mayer, and G. Gottschalk. 1987. Changes in the cell envelope structure of Clostridium sp. strain EM1 during massive production of α-amylase and pullulanase. FEMS Microbiol. Lett. 41:193-197.
2. Barrow, G. L., and R. K. A. Feltham. 1993. Cowan and Steel's manual for the identification of medical bacteria, 3rd ed. Cambridge University Press, Cambridge, United Kingdom.
3. Bishai, W. R., H. O. Smith, and G. J. Barcak. 1994. A peroxide/ascorbate-inducible catalase from Haemophilus influenzae is homologous to the Escherichia coli katE gene product. J. Bacteriol. 176:2914-2921.
4. Brosius, J., J. L. Palmer, J. P. Kennedy, and H. F. Noller. 1978. Complete nucleotide sequence of a 16S ribosomal RNA gene from Escherichia coli. Proc. Natl. Acad. Sci. USA 75:4801-4805.
5. Brown, S. M., M. L. Howell, M. L. Vasil, A. J. Anderson, and D. J. Hassett. 1995. Cloning and characterization of the katB gene of Pseudomonas aeruginosa encoding a hydrogen peroxide-inducible catalase: purification of KatB, cellular localization, and demonstration that it is essential for optimal resistance to hydrogen peroxide. J. Bacteriol. 177:6537-6544.
6. Ezaki, T., Y. Hashimoto, and E. Yabuuchi. 1989. Fluorometric deoxyribonucleic acid-deoxyribonucleic acid hybridization in microdilution well as an alternative to membrane filter hybridization in which radioisotopes are used to determine genetic relatedness among bacterial strains. Int. J. Syst. Bacteriol. 39:224-229.
7. Farr, S. B., and T. Kogoma. 1991. Oxidative stress responses in Escherichia coli and Salmonella typhimurium. Microbiol. Rev. 55:561-585.
8. Forsberg, C. W., T. J. Beveridge, and A. Hellstrom. 1981. Cellulase and xylanase release from Bacteroides succinogenes and its importance in the rumen environment. Appl. Environ. Microbiol. 42:886-896.
9. Gauthire, M. J., B. Lafay, R. Christen, L. Fernandez, M. Acquaviva, P. Bonin, and J.-C. Bertrand. 1992. Marinobacter hydrocarbonoclasticus gen. nov., sp. nov., a new, extremely halotolerant, hydrocarbon-degrading marine bacterium. Int. J. Syst. Bacteriol. 42:568-576.
10. Goldberg, I., and A. Hochman. 1989. Three different types of catalases in Klebsiella pneumoniae. Arch. Biochem. Biophys. 268:124-128.
11. González, J. M., F. Mayer, M. A. Moran, R. E. Hodoson, and W. B. Whitman. 1997. Microbulbifer hydrolyticus gen. nov., sp. nov., and Marinobacterium georgiense gen. nov., sp. nov., two marine bacteria from a lignin-rich pulp mill waste enrichment community. Int. J. Syst. Bacteriol. 47:369-376.
12. Gregory, E. M., and I. Fridorich. 1978. Visualization of catalase or acrylamide gels. Anal. Biochem. 58:57-62.
13. Hartford, O. M., and B. C. A. Dowds. 1994. Isolation and characterization of a hydrogen peroxide resistant strain of Bacillus subtilis. Microbiology 140: 297-304.
14. Hérouart, D., S. Sigaud, S. Moreau, P. Frendo, D. Touati, and A. Puppo. 1996. Cloning and characterization of the katA gene of Rhizobium meliloti encoding a hydrogen peroxide-inducible catalase. J. Bacteriol. 178:6802-6809.
15. Hicks, D. B. 1995. Purification of three catalase isozymes from facultatively alkaliphilic Bacillus firmus OF4. Biochim. Biophys. Acta 1299:347-355.
16. Hildebrandt, A. G., and I. Roots. 1975. Reduced nicotinamide adenine dinucleotide phosphate (NADPH)-dependent formation and breakdown of hydrogen peroxide during mixed function oxidation reaction in liver microsomes. Arch. Biochem. Biophys. 171:385-397.
17. Kim, H., J. S. Lee, Y. C. Hah, and J. H. Roe. 1994. Characterization of the major catalase from Streptomyces coelicolor ATCC 10147. Microbiology 140: 3391-3397.
18. Kimura, M. 1980. A simple method for estimating evolutionary rates of base substitution through comparative studies of nucleotide sequences. J. Mol. Evol. 16:111-120.
19. Klots, M. G., and S. W. Hutcheson. 1992. Multiple periplasmic catalases in phytopathogenic strains of Pseudomonas syringae. Appl. Environ. Microbiol. 58:2468-2473.
20. Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685.
21. Lee, J. S., Y. C. Hah, and J. H. Roe. 1993. The induction of oxidative enzymes in Streptomyces coelicolor upon hydrogen peroxide treatment. J. Gen. Microbiol. 139:1013-1018.
22. Leifson, E. 1963. Determination of carbohydrate metabolism of marine bacteria. J. Bacteriol. 85:1183-1184.
23. Loewen, P. C., J. Switala, and B. L. Triggs-Raine. 1985. Catalases HPI and HPII of Escherichia coli are induced independently. Arch. Biochem. Biophys. 243:144-149.
24. Lowry, O. H., N. J. Rosebrough, A. L. Farr, and R. J. Randall. 1951. Protein measurement with the Folin phenol reagent. J. Biol. Chem. 193:265-275.
25. Marmur, J. 1961. A procedure for the isolation of deoxyribonucleic acid from micro-organisms. J. Mol. Biol. 3:208-218.
26. Oppenheimer, C. H., and C. E. ZoBell. 1952. The growth and viability of sixty-three species of marine bacteria as influenced by hydrostatic pressure. J. Mar. Res. 11:10-18.
27. Ruimy, R., V. Breittmayer, P. Elbaze, B. Lafay, O. Boussemart, M. Gauthier, and R. Christen. 1994. Phylogenetic analysis and assessment of the genera Vibrio, Photobacterium, Aeromonas, and Plesiomonas deduced from small-subunit rRNA sequences. Int. J. Syst. Bacteriol. 44:416-426.
28. Satiou, N., and M. Nei. 1987. The neighbor-joining method: a new method for reconstructing phylogenetic trees. Mol. Biol. Evol. 4:406-425.
29. Sawabe, T., I. Sugimura, M. Ohtsuka, K. Nakano, K. Tajima, Y. Ezura, and R. Christen. 1998. Vibrio halioticoli sp. nov., a nonmotile alginolytic marine bacterium isolated from gut of abalone Haliotis diacus hannai. Int. J. Syst. Bacteriol. 48:573-580.
30. Tamaoka, J., and K. Komagata. 1984. Determination of DNA base composition by reversed-phase high-performance liquid chromatography. FEMS Microbiol. Lett. 25:125-128.
31. Thompson, J. D., D. G. Higgins, and T. J. Gibson. 1994. CLUSTAL W: improving the sensitivity of progressive multiple sequence weighing, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 76: 4350-4354.
32. Wang, H., Y. Tokusige, H. Shinoyama, T. Fujii, and T. Urakami. Purification and characterization of thermostable catalase from culture broth of Thermoascus aurantiacus. J. Ferment. Bioeng. 85:169-173.
33. Yumoto, I., K. Yamazaki, K. Kawasaki, N. Ichise, N. Morita, T. Hoshino, and H. Okuyama. 1998. Isolation of Vibrio sp. S-1 exhibiting extraordinarily high catalase activity. J. Ferment. Bioeng. 85:113-116.