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Role of oxygen radicals in the bacteriostatic effect of whey and production of bacterial growth by free radical scavengers

Published online by Cambridge University Press:  01 June 2009

Tiina Mattila
Affiliation:
Department of Pharmacology and Toxicology, College of Veterinary Medicine, 00550 Helsinki 55, Finland

Summary

The involvement of toxic oxygen intermediates in the bacteriostatic effect of milk was determined by producing bacterial growth curves using turbidimetry in the presence and absence of oxygen radical-scavenging substances. Using whey as substrate, catalase, haemoglobin combined with ascorbic acid and xanthine oxidase inhibitors all provided protection against oxygen toxicity for a strain of Staphylococcus aureus and of Streptococcus agalactiae. Superoxide dismutase and mannitol were less effective. This was evident in whey alone and in the presence of oxygen radicals produced exogenously by the t-butylhydroperoxide, H2O2 and xanthine/xanthine oxidase systems.

Type
Original Articles
Copyright
Copyright © Proprietors of Journal of Dairy Research 1985

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References

REFERENCES

Auclair, J. & Vassal, Y. 1963 Occurrence of variants sensitive to agglutinins and to lactoperoxidase in a lactenin-resistant strain of Streptococcus lactis. Journal of Dairy Research 30 345349CrossRefGoogle Scholar
Aurand, L. W., Boone, N. H. & Giddings, G. G. 1977 Superoxide and singlet oxygen in milk lipid peroxidation. Journal of Dairy Science 60 363369.CrossRefGoogle Scholar
Babior, B. M., Curnutte, J. T. & Kipnes, R. S. 1975 Biological defense mechanisms. Evidence for the participation of superoxide in bacterial killing by xanthine oxidase. Journal of Laboratory and Clinical Medicine 85 235244Google Scholar
Battelli, M. G., Lorenzoni, E. & Stirpe, F. 1973 Milk xanthine oxidase type D (dehydrogenase) and type O (oxidase). Purification, interconversion and some properties. Biochemical Journal 131 191198Google Scholar
Brawn, K. & Fridovich, I. 1980 Superoxide radical and superoxide dismutases: threat and defense. Acta Physiologica Scandinavica Supplementum 492 918Google Scholar
Briley, M. S. & Eisenthal, R. 1974 Association of xanthine oxidase with the bovine milk-fat-globule membrane. Catalytic properties of the free and membrane-bound enzyme. Biochemical Journal 143 149157.CrossRefGoogle ScholarPubMed
Chatterjee, I. B. 1978 Ascorbic acid metabolism. World Review of Nutrition and Dietetics 30 6987Google Scholar
Deeth, H. C. 1983 Homogenized milk and atherosclerotic disease: a review. Journal of Dairy Science 66 14191435CrossRefGoogle ScholarPubMed
Del Maestro, R. F. 1980 An approach to free radicals in medicine and biology. Acta Physiologica Scandinavica Supplementum 492 153168Google Scholar
Del Maestro, R. F., Thaw, H. H., Björk, J., Planker, M. & Arfors, K.-E. 1980 Free radicals as mediators of tissue injury. Acta Physiologica Scandinavica Supplementum 492 4357Google ScholarPubMed
Dormandy, T. L. 1983 An approach to free radicals. Lancet ii 10101014CrossRefGoogle ScholarPubMed
Evelyn, K. A. & Malloy, H. T. 1938 Mierodetermination of oxyhemoglobin, methemoglobin, and sulf- hemoglobin in a single sample of blood. Journal of Biological Chemistry 126 655662CrossRefGoogle Scholar
Fox, I. H. 1978 Degradation of purine nucleotides in uric acid. Handbuch der Experimentellen Pharmakologie 51 93124Google Scholar
Fridovich, I. 1983 Superoxide radical: an endogenous toxicant. Annual Review of Pharmacology and Toxicology 23 239257CrossRefGoogle ScholarPubMed
Gregory, E. M., Yost, F. J. & Fridovich, I. 1973 Superoxide dismutases of Escherichia coli: intracellular localization and functions. Journal of Bacteriology 115 987991Google Scholar
Haber, F. & Weiss, J. 1934 The catalytic decomposition of hydrogen peroxide by iron salts. Proceedings of the Royal Society of London A 147 332351Google Scholar
Hill, R. D. 1979 Oxidative enzymes and oxidative processes in milk. CSIRO Food Research Quarterly 39 3337Google Scholar
Johnson, A. H. 1974 The composition of milk. In Fundamentals of Dairy Chemistry 2nd edn pp. 3539 (Eds Webb, B. H., Johnson, A. H. and Alford, J. A.). Westport, CT: Avi Publishing Co. Inc.Google Scholar
Karnovsky, M. L. & Badwey, J. A. 1983 Determinants of the production of active oxygen species by granulocytes and macrophages. Journal of Clinical Chemistry and Clinical Biochemistry 21 545553Google ScholarPubMed
Kellogg, E. W. & Fridovich, I. 1975 Superoxide, hydrogen peroxide and singlet oxygen in lipid peroxidation by a xanthine oxidase system. Journal of Biological Chemistry 250 88128817Google Scholar
Klastrup, O. 1975 Scandinavian recommendations on examination of quarter milk samples. International Dairy Federation Annual Bulletin Document 85 4952Google Scholar
Maisi, P., Mattila, T. & Sandholm, M. 1983 Heme-iron and ecology of Escherichia coli within the porcine gut. Comparative Immunology and Microbiology of Infectious Diseases 6 273280Google Scholar
Maisi, P., Mattila, T. & Sandholm, M. 1984 Effect of milk fat globule membrane reversing heme-stimulated bacterial growth in whey. Journal of Dairy Science in pressCrossRefGoogle Scholar
Mangino, M. E. & Brunner, J. R. 1977 Isolation and partial characterization of xanthine oxidase associated with the milk fat globule membrane of cows' milk. Journal of Dairy Science 60 841850Google Scholar
Mattila, T., Maisi, P. & Sandholm, M. 1984 Haem compounds as growth promoters in whey - a possible bacterial application to bovine mastitis. Research in Veterinary Science 36 5256CrossRefGoogle ScholarPubMed
Michelson, A. M. & Buckingham, M. E. 1974 Effects of superoxide radicals on myoblast growth and differentiation. Biochemical and Biophysical Research Communications 58 10791086CrossRefGoogle ScholarPubMed
Oram, J. D. & Reiter, B. 1966 The inhibition of streptococci by lactoperoxidase, thiocyanate and hydrogen peroxide. The effect of the inhibitory system on susceptible and resistant strains of group N streptococci. Biochemical Journal 100 373381CrossRefGoogle ScholarPubMed
Pedersen, T. C. & Aust, S. D. 1973 The role of superoxide and singlet oxygen in lipid peroxidation promoted by xanthine oxidase. Biochemical and Biophysical Research Communications 52 10711078Google Scholar
Reiter, B. 1979 The lactoperoxidase–thiocyanate–hydrogen peroxide antibacterium system. In Oxygen Free Radicals and Tissue damage pp. 285294. Amsterdam: Excerpta Medica (Ciba Foundation Symposium 65)Google Scholar
Reiter, B. & Oram, J. D. 1967 Bacterial inhibitors in milk and other biological fluids. Nature 216 328330Google Scholar
Rosen, H. & Klebanoff, S. J. 1977 Formation of singlet oxygen by the myeloperoxidase-mediated antimicrobial system. Journal of Biological Chemistry 252 48034810Google Scholar
Simmons, S. R. & Karnovsky, M. L. 1973 Iodinating ability of various leukocytes and their bactericidal activity. Journal of Experimental Medicine 138 4463CrossRefGoogle ScholarPubMed
Strauss, R. R., Paul, B. B., Jacobs, A. A. & Sbarra, A. J. 1971 Role of the phagocyte in host–parasite interactions. XXVII. Myeloperoxidase-H2O2-Cl--mediated aldehyde formation and its relationship to antimicrobial activity. Infection and Immunity 3 595602CrossRefGoogle ScholarPubMed
Suovaniemi, O. & Jarnefelt, J. 1982 Discrete multichannel analysis system. International Laboratory April 4860Google Scholar
Van Hemmen, J. J. & Meuling, W. J. A. 1975 Inactivation of biologically active DNA by γ-ray-induced superoxide radicals and their dismutation products: singlet molecular oxygen and hydrogen peroxide. Biochimica et Biophysica Acta 402 133141Google Scholar