This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Yumoto, I.
Right arrow Articles by Kawasaki, K.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Yumoto, I.
Right arrow Articles by Kawasaki, K.

 Previous Article  |  Next Article 

Journal of Bacteriology, April 2000, p. 1903-1909, Vol. 182, No. 7
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Purification and Characterization of a Catalase from the Facultatively Psychrophilic Bacterium Vibrio rumoiensis S-1T Exhibiting High Catalase Activity

Isao Yumoto,1,* Daisen Ichihashi,1 Hideaki Iwata,1,2 Anita Istokovics,1,3,dagger Nobutoshi Ichise,1,3 Hidetoshi Matsuyama,2 Hidetoshi Okuyama,1,3 and Kosei Kawasaki1

Bioscience and Chemistry Division, Hokkaido National Industrial Research Institute, Tsukisamu-Higashi, Toyohira-ku, Sapporo 062-8517,1 Department of Bioscience and Technology, School of Engineering, Hokkaido Tokai University, Minaminosawa, Minami-ku, Sapporo 005-8601,2 and Laboratory of Environmental Molecular Biology, Graduate School of Environmental Earth Science, Hokkaido University, Sapporo 060-0810,3 Japan

Received 8 July 1999/Accepted 7 January 2000

Catalase from the facultatively psychrophilic bacterium Vibrio rumoiensis S-1T, which was isolated from an environment exposed to H2O2 and exhibited high catalase activity, was purified and characterized, and its localization in the cell was determined. Its molecular mass was 230 kDa, and the molecule consisted of four identical subunits. The enzyme, which was not apparently reduced by dithionite, showed a Soret peak at 406 nm in a resting state. The catalytic activity was 527,500 U · mg of protein-1 under standard reaction conditions at 40°C, 1.5 and 4.3 times faster, respectively, than those of the Micrococcus luteus and bovine catalases examined under the same reaction conditions, and showed a broad optimum pH range (pH 6 to 10). The catalase from strain S-1T is located not only in the cytoplasmic space but also in the periplasmic space. There is little difference in the activation energy for the activity between strain S-1T catalase and M. luteus and bovine liver catalases. The thermoinstability of the activity of the former catalase were significantly higher than those of the latter catalases. The thermoinstability suggests that the catalase from strain S-1T should be categorized as a psychrophilic enzyme. Although the catalase from strain S-1T is classified as a mammal type catalase, it exhibits the unique enzymatic properties of high intensity of enzymatic activity and thermoinstability. The results obtained suggest that these unique properties of the enzyme are in accordance with the environmental conditions under which the microorganism lives.

* Corresponding author. Mailing address: 2-17-2-1 Tsukisamu-Higashi, Toyohira-ku, Sapporo 062-8517, Japan. Phone: 81-11-857-8925. Fax: 81-11-857-8900. E-mail: yumoto{at}hniri.go.jp.

dagger Present address: Institute of Plant Biology Biological Research Center, Hungarian Academy of Sciences Temesvari krt. 62, H-6701 Szeged, Hungary.

Journal of Bacteriology, April 2000, p. 1903-1909, Vol. 182, No. 7
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Mailloux, R. J., Singh, R., Brewer, G., Auger, C., Lemire, J., Appanna, V. D. (2009). {alpha}-Ketoglutarate Dehydrogenase and Glutamate Dehydrogenase Work in Tandem To Modulate the Antioxidant {alpha}-Ketoglutarate during Oxidative Stress in Pseudomonas fluorescens. J. Bacteriol. 191: 3804-3810 [Abstract] [Full Text]  
  • Chenier, D., Beriault, R., Mailloux, R., Baquie, M., Abramia, G., Lemire, J., Appanna, V. (2008). Involvement of Fumarase C and NADH Oxidase in Metabolic Adaptation of Pseudomonas fluorescens Cells Evoked by Aluminum and Gallium Toxicity. Appl. Environ. Microbiol. 74: 3977-3984 [Abstract] [Full Text]  
  • Park, K.-J., Kang, M.-J., Kim, S. H., Lee, H.-J., Lim, J.-K., Choi, S. H., Park, S.-J., Lee, K.-H. (2004). Isolation and Characterization of rpoS from a Pathogenic Bacterium, Vibrio vulnificus: Role of {sigma}S in Survival of Exponential-Phase Cells under Oxidative Stress. J. Bacteriol. 186: 3304-3312 [Abstract] [Full Text]  
  • Ohtani, N., Haruki, M., Morikawa, M., Kanaya, S. (2001). Heat labile ribonuclease HI from a psychrotrophic bacterium: gene cloning, characterization and site-directed mutagenesis. Protein Eng Des Sel 14: 975-982 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»