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Bioscience, Biotechnology, and Biochemistry Volume 72, 2008 - Issue 10
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Original Articles

Hydrogen Peroxide Resistance of Acetobacter pasteurianus NBRC3283 and Its Relationship to Acetic Acid Fermentation

Akiko OKAMOTO-KAINUMADepartment of Fermentation Science, Tokyo University of Agriculture
,
Yasunori EHATADepartment of Fermentation Science, Tokyo University of Agriculture
,
Manami IKEDADepartment of Fermentation Science, Tokyo University of Agriculture
,
Takemasa OSONODepartment of Fermentation Science, Tokyo University of Agriculture
,
Morio ISHIKAWADepartment of Fermentation Science, Tokyo University of Agriculture
,
Takayuki KAGACentral Research Institute, Mizkan Group Corporation
&
Yukimichi KOIZUMIDepartment of Fermentation Science, Tokyo University of Agriculture
 show all
Pages 2526-2534 | Received 05 Mar 2008, Accepted 23 Jun 2008, Published online: 22 May 2014

  • 1) Ameyama, M., and Adachi, O., Alcohol dehydrogenase from acetic acid bacteria, membrane-bound. Methods Enzymol., 89, 450–457 (1982).
  • 2) Ameyama, M., and Adachi, O., Aldehyde dehydrogenase from acetic acid bacteria, membrane-bound. Methods Enzymol., 89, 491–497 (1982).
  • 3) Sievers, M., and Swings, J., Genus I. Acetobacter Beijerinck 1898, 215.AL In “Bergey’s Manual of Systematic Bacteriology” 2nd ed. Vol. 2, eds. Brenner, D. J., Krieg, N. R., and Staley, J. T., Springer, New York, pp. 51–54 (2005).
  • 4) Fridovich, I., The biology of oxygen radicals. Science, 201, 875–880 (1978).
  • 5) Schellhorn, H. E., Regulation of hydroperoxidase (catalase) expression in Escherichia coli. FEMS Microbiol. Lett., 131, 113–119 (1995).
  • 6) Tsung, H., McEwan, A. G., Apicella, M. A., and Jennings, M. P., OxyR acts as a repressor of catalase expression in Neisseria gonorrhoeae. Infect. Immun., 71, 550–556 (2003).
  • 7) Park, K.-J., Kang, M.-J., Kim, S. H., Lee, H.-J., Lim, J.-K., Choi, S.-H., Park, S.-J., and Lee, K.-H., Isolation and characterization of rpoS from a pathogenic bacterium, Vibrio vulnificus: role of σs in survival of exponential-phase cells under oxidative stress. J. Bacteriol., 186, 3304–3312 (2004).
  • 8) Sambrook, J., and Russell, D. W., “Molecular Cloning, a Laboratory Manual” 3rd edn., Cold Spring Harbor Laboratory, Cold Spring Harbor (2001).
  • 9) Okamoto-Kainuma, A., Wang, Y., Kadono, S., Tayama, K., Koizumi, Y., and Yanagida, F., Cloning and characterization of groESL operon in Acetobacter aceti. J. Biosci. Bioeng., 94, 140–147 (2002).
  • 10) Vattanaviboon, P., and Mongkolsak, S., Expression analysis and characterization of the mutant of a growth-phase- and starvation-regulated monofunctional catalase gene from Xanthomonas campestris pv. phaseoli. Gene, 241, 259–265 (2000).
  • 11) Bradford, M. M., A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein dye binding. Anal. Biochem., 72, 248–254 (1976).
  • 12) Wayne, L. G., and Diaz, G. A., A double staining method for differentiating between two classes of mycobacerial catalase in polyacrylamide electrophoresis gels. Anal. Biochem., 157, 89–92 (1986).
  • 13) Clare, D., Duong, M. N., Darr, D., Archibald, F., and Fridovich, I., Effects of molecular oxygen on detection of superoxide radical with nitroblue tetrazolium and on activity stains for catalase. Anal. Biochem., 140, 532–537 (1984).
  • 14) Schell, M. A., Molecular biology of the LysR family of transcriptional regulators. Annu. Rev. Microbiol., 47, 597–626 (1993).
  • 15) Zheng, M., Aslund, F., and Storz, G., Activation of the OxyR transcription factor by reversible disulfide bond formation. Science, 279, 1718–1722 (1998).
  • 16) Saeki, A., Taniguchi, M., Matsushita, K., Toyama, H., Theeragool, G., Lotong, N., and Adachi, O., Microbiological aspects of acetate oxidation by acetic acid bacteria, unfavorable phenomena in vinegar fermentation. Biosci. Biotechnol. Biochem., 61, 317–323 (1997).
  • 17) Matsushita, K., Shinagawa, E., Adachi, O., and Ameyama, M., Purification, characterization and reconstitution of cytochrome o-type oxidase from Gluconobacter suboxydans. Biochim. Biophys. Acta, 894, 304–312 (1987).
  • 18) Matsushita, K., Nonobe, M., Shinagawa, E., Adachi, O., and Ameyama, M., Reconstitution of pyrroloquinoline quinine-dependent D-glucose oxidase respiratory chain of Escherichia coli with cytochrome o oxidase. J. Bacteriol., 169, 205–209 (1987).
  • 19) González-Flacha, B., and Demple, B., Genetic responses to free radicals: homeostasis and gene control. Ann. NY Acad. Sci., 899, 69–87 (2000).
  • 20) Miyoshi, A., Rochat, T., Gratadoux, J.-J., Loir, Y. L., Oliveira, S. C., Langella, P., and Azevedo, V., Oxidative stress in Lactococcus lactis. Genet. Mol. Res., 2, 348–359 (2003).
  • 21) Niimura, Y., Nishiyama, Y., Saito, D., Tsuji, H., Hidaka, M., Miyaji, T., Watanabe, T., and Massey, V., A hydrogen peroxide-forming NADH oxidase that functions as an alkyl hydroperoxidase reductase in Amphibacillus xylans. J. Bacteriol., 182, 5046–5051 (2000).
  • 22) Luo, L., Qi, M.-S., Yao, S.-Y., Cheng, H.-P., Zhu, J.-B., and Yu, G.-Q., Role of oxyR from Sinorhizobium meliloti in regulating the expression of catalases. Acta Biochim. Biophys. Sin., 37, 421–428 (2005).
  • 23) Kim, J., and Mayfield, J., Identification of Brucella abortus OxyR and its role in control of catalase expression. J. Bacteriol., 182, 5631–5633 (2000).
  • 24) del Carmen Vargas, M., Encarnación, S., Dávalos, A., Reyes-Pérez, A., Mora, Y., García-de los Santos, A., Brom, S., and Mora, J., Only one catalase, katG, is detectable in Rhizobium etli, and is encoded along with the regulator OxyR on a plasmid replicon. Microbiology, 149, 1165–1176 (2003).
  • 25) Ameyama, M., Biochemistry and biotechnology concerning vinegar. In “Su no Kagaku” (in Japanese), eds. Ameyama, M., and Otsuka, S., Asakura Publishing, Tokyo, pp. 121–122 (1990).

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