Skip to main content
NCBI home page
Applied and Environmental Microbiology logoLink to Applied and Environmental Microbiology
. 1981 Feb;41(2):449–454. doi: 10.1128/aem.41.2.449-454.1981

Superoxide dismutase activity in thermally stressed Staphylococcus aureus.

E R Bucker, S E Martin
PMCID: PMC243714  PMID: 7235693

Abstract

The effects of heat and NaCl on the activity of superoxide dismutase from Staphylococcus aureus were examined. A linear decrease in superoxide dismutase activity occurred when S. aureus MF-31 cells were thermally stressed for 90 min at 52% C in 100 mM potassium phosphate buffer (pH 7.2). After 20 min of heating, only 5% of the superoxide dismutase activity was lost. Heating for 60, 90 and 120 min resulted in decreases of approximately 10, 22, and 68%, respectively. The rates of thermal inactivation of superoxide dismutase from S. aureus strains 196E and 210 were similar and slightly greater than those of strains MF-31, S-6, and 181. The addition of NaCl before or after heating resulted in increased losses of superoxide dismutase activity.

Full text

PDF
449

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Andrews G. P., Martin S. E. Catalase activity during the recovery of heat-stressed Staphylococcus aureus MF-31. Appl Environ Microbiol. 1979 Sep;38(3):390–394. doi: 10.1128/aem.38.3.390-394.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Andrews G. P., Martin S. E. Heat inactivation of catalase from Staphylococcus aureus MF-31. Appl Environ Microbiol. 1979 Jun;37(6):1180–1185. doi: 10.1128/aem.37.6.1180-1185.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Brewer D. G., Martin S. E., Ordal Z. J. Beneficial effects of catalase or pyruvate in a most-probable-number technique for the detection of Staphylococcus aureus. Appl Environ Microbiol. 1977 Dec;34(6):797–800. doi: 10.1128/aem.34.6.797-800.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Flowers R. S., Martin S. E., Brewer D. G., Ordal Z. J. Catalase and enumeration of stressed Staphylococcus aureus cells. Appl Environ Microbiol. 1977 May;33(5):1112–1117. doi: 10.1128/aem.33.5.1112-1117.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Forman H. J., Fridovich I. On the stability of bovine superoxide dismutase. The effects of metals. J Biol Chem. 1973 Apr 25;248(8):2645–2649. [PubMed] [Google Scholar]
  6. Frey H. E., Pollard E. C. Ionizing radiation and bacteria: nature of the effect of irradiated medium. Radiat Res. 1966 Jul;28(3):668–676. [PubMed] [Google Scholar]
  7. Hurst A., Hendry G. S., Hughes A., Paley B. Enumeration of sublethally heated staphylococci in some dried foods. Can J Microbiol. 1976 May;22(5):677–683. doi: 10.1139/m76-100. [DOI] [PubMed] [Google Scholar]
  8. Iandolo J. J., Ordal Z. J. Repair of thermal injury of Staphylococcus aureus. J Bacteriol. 1966 Jan;91(1):134–142. doi: 10.1128/jb.91.1.134-142.1966. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Keele B. B., Jr, McCord J. M., Fridovich I. Superoxide dismutase from escherichia coli B. A new manganese-containing enzyme. J Biol Chem. 1970 Nov 25;245(22):6176–6181. [PubMed] [Google Scholar]
  10. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  11. Martin S. E., Flowers R. S., Ordal Z. J. Catalase: its effect on microbial enumeration. Appl Environ Microbiol. 1976 Nov;32(5):731–734. doi: 10.1128/aem.32.5.731-734.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. McCord J. M., Fridovich I. Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein). J Biol Chem. 1969 Nov 25;244(22):6049–6055. [PubMed] [Google Scholar]
  13. Przybylski K. S., Witter L. D. Injury and recovery of Escherichia coli after sublethal acidification. Appl Environ Microbiol. 1979 Feb;37(2):261–265. doi: 10.1128/aem.37.2.261-265.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Ray B., Speck M. L. Freeze-injury in bacteria. CRC Crit Rev Clin Lab Sci. 1973 Aug;4(2):161–213. doi: 10.3109/10408367309151556. [DOI] [PubMed] [Google Scholar]
  15. Rigo A., Stevanato R., Viglino P. Competitive inhibition of Cu, Zn superoxide dismutase by monovalent anions. Biochem Biophys Res Commun. 1977 Dec 7;79(3):776–783. doi: 10.1016/0006-291x(77)91179-2. [DOI] [PubMed] [Google Scholar]
  16. Rigo A., Viglino P., Rotilio G., Tomat R. Effect of ionic strength on the activity of bovine superoxide dismutase. FEBS Lett. 1975 Jan 15;50(1):86–88. doi: 10.1016/0014-5793(75)81047-7. [DOI] [PubMed] [Google Scholar]
  17. Roth L. A., Keenan D. Acid injury of Escherichia coli. Can J Microbiol. 1971 Aug;17(8):1005–1008. doi: 10.1139/m71-160. [DOI] [PubMed] [Google Scholar]
  18. Scheusner D. L., Busta F. F., Speck M. L. Injury of bacteria by sanitizers. Appl Microbiol. 1971 Jan;21(1):41–45. doi: 10.1128/am.21.1.41-45.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Vance P. G., Keele B. B., Jr, Rajagopalan K. V. Superoxide dismutase from Streptococcus mutans. Isolation and characterization of two forms of the enzyme. J Biol Chem. 1972 Aug 10;247(15):4782–4786. [PubMed] [Google Scholar]

Articles from Applied and Environmental Microbiology are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES