Thermostable Peroxidase from Free

Abstract

A peroxidase from was purified to homogeneity. The enzyme ( 175000) was composed of two subunits of equal size, and showed a Soret band at 406 nm. On reduction with sodium dithionite, absorption at 434 nm and 558 nm was observed. The spectrum of reduced pyridine haemochrome showed peaks at 418, 526 and 557 nm; the reduced oxidized spectrum of pyridine haemochrome showed peaks of 418, 524 and 556 nm with a trough at 452 nm. These results indicate that the enzyme contained protohaem IX as a prosthetic group. The optimum pH was about 6 and the apparent optimum temperature was 70 °C. The enzyme was relatively stable up to 70 °C; at 30 °C it was stable for a month. The enzyme had peroxidase activity toward a mixture of 2,4-dichlorophenol and 4-aminoantipyrine with a for HO of 1·3 m. It also acted as a catalase with a for HO of 7·5 m.

Loading

Article metrics loading...

/content/journal/micro/10.1099/00221287-134-7-1971
1988-07-01
2024-03-28
Loading full text...

Full text loading...

/deliver/fulltext/micro/134/7/mic-134-7-1971.html?itemId=/content/journal/micro/10.1099/00221287-134-7-1971&mimeType=html&fmt=ahah

References

  1. Aebi H. 1983; Catalase. In Methods of Enzymatic Analysis 616, 3rd edn. pp. 273–285 Bergmeyer H. U. Edited by Weinheim: Verlag Chemie;
    [Google Scholar]
  2. Brill A. S. 1966; Peroxidase and catalase. In Comprehensive Biochemistry 617: pp. 447–449 Florkin M., Stotz E. H. Edited by Amsterdam: Elsevier;
    [Google Scholar]
  3. Claiborne A., Fridovich I. 1979; Purification of the o-dianisidine peroxidase from Escherichia coli B. Physicochemical characterization and analysis of its dual catalatic and peroxidatic activities. Journal of Biological Chemistry 254:4245–4252
    [Google Scholar]
  4. Clayton R. K. 1959; Purified catalase from Rhodo- pseudomonas sphaeroides. Biochimica et biophysica acta 36:40–47
    [Google Scholar]
  5. Davis B. J. 1964; Disc electrophoresis 11. Methods and application to human serum proteins. Annals of the New York Academy of Sciences 121:404–408
    [Google Scholar]
  6. Dolin M. I. 1957; Streptococcus faecelis oxidase for reduced diphosphopyridine nucleotide. Journal of Biological Chemistry 225:557–573
    [Google Scholar]
  7. Emerson J. 1943; The condensation of aminoanti- pyrine II. A new color test for phenolic compounds. Journal of Organic Chemistry 8:417–428
    [Google Scholar]
  8. Falk J. E. 1964a Porphyrins and Metalloporphyrins pp. 181–182 New York: Elsevier;
    [Google Scholar]
  9. Falk J. E. 1964b Porphyrins and Metalloporphyrins pp. New York: Elsevier;
    [Google Scholar]
  10. Finzel B. C., Poulos T. L., Kraut J. 1984; Crystal structure of yeast cytochrome c peroxidase refined at 1·7 A resolution. Journal of Biological Chemistry 259:13027–13036
    [Google Scholar]
  11. Fukumori Y., Fujiwara T., Okuda-Tahahashi Y., Mukohata Y., Yamanaka T. 1985; Purification and properties of a peroxidase from Halobacterium halobium L-33. Journal of Biochemistry 98:1055–1061
    [Google Scholar]
  12. Gregory E. M., Fridovich I. 1974; Visualization of catalase on acrylamide gels. Analytical Biochemistry 58:57–62
    [Google Scholar]
  13. Herbert D., Pinsent J. 1948; Crystalline bacterial catalase. Biochemical Journal 43:193–202
    [Google Scholar]
  14. Hildebrandt A. G., Roots I. 1975; Reduced nicotinamide adenine dinucleotide phosphate (NADPH)-dependent formation and breakdown of hydrogen peroxide during mixed function oxidation reduction in liver microsomes. Archives of Biochemistry and Biophysics 171:385–397
    [Google Scholar]
  15. Hochman A., Shemesh A. 1987; Purification and characterization of a catalase-peroxidase from the photosynthetic bacterium Rhodopseudomonas capsu- lata. Journal of Biological Chemistry 264:6871–6876
    [Google Scholar]
  16. Ichikawa K., Okazaki K., Kimoto K., Watan-Abe Y. 1981; Partial purification of peroxidase from Pellicularia filamentosa. Agricultural and Biological Chemistry 45:1297–1299
    [Google Scholar]
  17. Lenhoff H. M., Kaplan N. O. 1956; A cytochrome peroxidase from Pseudomonas fluores- cens. Journal of Biological Chemistry 220:967–982
    [Google Scholar]
  18. Loewen P. C., Triggs B. L. 1984; Genetic mapping of katF, a new locus that with katE affects the synthesis of a second catalase species in Escherichia coli. Journal of Bacteriology 160:668–695
    [Google Scholar]
  19. Nadler V., Goldberg I., Hochman A. 1986; Comparative study of bacterial catalases. Biochimica et biophysica acta 882:234–241
    [Google Scholar]
  20. Nies D., Schlegel H. G. 1982; Catalase from Comamonas compransoris. Journal of General and Applied Microbiology 28:311–319
    [Google Scholar]
  21. PAUL K. G. 1963; Peroxidases. In The Enzyme 8 pp. 227–274 Boyer P. D., Lardy H. A., Myrback K. Edited by New York: Academic Press;
    [Google Scholar]
  22. Poole R. K., Baines B. S., Appleby A. C. 1986; Haemoprotein 6-590(Escherichia coli), a reducible catalase and peroxidase: evidence for its close relationship to hydroperoxidase I and cytochrome a] b preparation. Journal of General Microbiology 132:1525–1539
    [Google Scholar]
  23. Putter J., Becker R. 1983; Peroxidases. In Methods of Enzymatic Analysis 3, 3rd edn. pp. 286–292 Bergmeyer H. U. Edited by Weinheim: Verlag Chemie;
    [Google Scholar]
  24. Shinmen Y., Asami S., Amachi T., Shimizu S., Yamada H. 1986; Crystallization and characterization of an extracellular fungal peroxidase. Agricultural and Biological Chemistry 50:247–249
    [Google Scholar]
  25. Tamaoku K., Murao Y., Akiura K., Ohkura Y. 1982; New water soluble hydrogen donors for the enzymatic spectrophotometric determination of hydrogen peroxide. Analytica chimica acta 136:121–127
    [Google Scholar]
  26. Weber & Osborn K. 1969; The reliability of molecular weight determination by dodecyl sulfate polyacrylamide gel electrophoresis. Journal of Biological Chemistry 244:4406–4409
    [Google Scholar]
  27. Welinder K. G. 1979; Amino acid sequence studies of horseradish peroxidase. European Journal of Biochemistry 96:483–502
    [Google Scholar]
http://instance.metastore.ingenta.com/content/journal/micro/10.1099/00221287-134-7-1971
Loading
/content/journal/micro/10.1099/00221287-134-7-1971
Loading

Data & Media loading...

Most cited Most Cited RSS feed