Hostname: page-component-745bb68f8f-mzp66 Total loading time: 0 Render date: 2025-01-22T03:48:13.809Z Has data issue: false hasContentIssue false
  • English
  • Français

Influence of milk proteins on lipid oxidation in aqueous emulsion: II. Lactoperoxidase, lactoferrin, superoxide dismutase and xanthine oxidase

Published online by Cambridge University Press:  01 June 2009

John C. Allen  and
Wendy L. Wrieden
John C. Allen
Affiliation:
Research Division, North E. Wales Institute, Kelsterton College, Connah's Quay, Deeside, Clwyd, UK
Wendy L. Wrieden
Affiliation:
Research Division, North E. Wales Institute, Kelsterton College, Connah's Quay, Deeside, Clwyd, UK
Get access Rights & Permissions [Opens in a new window]

Summary

The milk-related model system described by Allen & Wrieden (1982) was used to assess the effects of a number of purified milk metalloproteins, at concentrations relevant to those in milk and dairy products, on triglyceride oxidation in emulsions. Oxidations were monitored by the rate of O2 utilization (ROU) and by the thiobarbituricacid (TBA) assay. The proteins lactoferrin, lactoperoxidase, superoxide dismutase and xanthine oxidase were used either on their own or in conjunction with 10 μM-Cu2+ or Fe2+. Lactoferrin alone had little effect on oxidation, although both the iron-free and iron-saturated protein were able to protect the lipid to some extent from Fe2+-catalysed oxidation. Cu2+-catalysed oxidation was slightly promoted. Lactoperoxidase was pro-oxidative in the absence and presence of added Cu2+ or Fe2+. Heat treatment at 72°C/20 s had little effect, but oxidation was greatly reduced by treatment at 80°C/20 s. Superoxide dismutase strongly reduced the rate of lipid oxidation in the absence of added metals, but had no effect in the presence of 10 μM-Cu2+. xanthine oxidase had little effect on lipid oxidation in the absence of added metals, but was strongly pro-oxidative in the presence of 10 μ-Cu2+. Similar effects were observed down to 1 μM-Cu2+. The enzymic activity of xanthine oxidase was rapidly eliminated by 10 μM-Cu2+, but not by 10 μM-Fe2+. A moderate pro-oxidative effect was observed in the presence of 10 μM-Fe2+. Heat treatment of xanthine oxidase at 80°C/20 s reduced its lipid pro-oxidative effect in the presence of Cu2+ more effectively than treatment at 72°C/20 s.

Type
Original Articles
Information
Journal of Dairy Research , Volume 49 , Issue 2 , May 1982 , pp. 249 - 263
Copyright
Copyright © Proprietors of Journal of Dairy Research 1982

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

REFERENCES

Allen, J. C. & Farag, R. S. 1973 A comparison between the metal-catalysed oxidation of aqueous emulsions of linoleic acid, trilinolein and phospholipids. Proceedings of the 3rd International Symposium on Metal-Catalysed Lipid Oxidation pp. 44–56Paris: Institut des Corps GrasGoogle Scholar
Allen, J. C., Farag, R. S. & Crook, E. M. 1979 The metal-catalysed oxidation of aqueous emulsions of linoleic acid and trilinolein. Journal of Applied Biochemistry 1 1–15Google Scholar
Allen, J. C. & Humphries, C. 1975 The use of zwitterionic surfactants in the agarose chromatography of biological membranes. FEBS Letters 57 158–162CrossRefGoogle ScholarPubMed
Allen, J. C. & Humphries, C. 1977 The oxidation of lipids by components of bovine milk-fat globule membrane. Journal of Dairy Research 44 495–507CrossRefGoogle Scholar
Allen, J. C. & Wrieden, W. L. 1982 The influence of milk proteins on lipid oxidation in aqueous emulsion I. Casein, whey protein and α-lactalbumin. Journal of Dairy Research 49 239–248CrossRefGoogle Scholar
Asada, K. 1976 Occurrence of superoxide dismutase in bovine milk. Agricultural and Biological Chemistry 40 1659–1660Google Scholar
Aurand, L. W., Boone, N. H. & Giddings, G. G. 1977 Superoxide and singlet oxygen in milk lipid peroxidation. Journal of Dairy Science 60 363–369CrossRefGoogle Scholar
Aurand, L. W. & Woods, A. E. 1959 Role of xanthine oxidase in the development of spontaneously oxidized flavor in milk. Journal of Dairy Science 42 1111–1118CrossRefGoogle Scholar
Bergel, F. & Bray, R. C. 1959 The chemistry of xanthine oxidase. 4. The problems of enzyme inactivation and stabilization. Biochemical Journal 73 182–192CrossRefGoogle Scholar
Beromeyer, H. U., Gawehn, K. & Grassl, M. 1974 Enzymes as biochemical reagents. Methods of Enzymatic Analysis 2nd Edn Vol. 1 p. 495. (Ed. Bergmeyer, H. U.) New York: Academic PressGoogle Scholar
Bors, W., Michel, C. & Saran, M. 1979 Superoxide anions do not react with hydroperoxides. FEBS Letters 107 403–406CrossRefGoogle Scholar
Bray, R. C. 1975 Molybdenum iron-sulfur flavin hydroxylases and related enzymes. In The Enzymes (Ed. Boyer, P. D.) 3rd Edn Vol. XIIB pp. 299–419. New York: Academic PressGoogle Scholar
Cerbulis, J. & Farrell, H. M. 1977 Xanthine oxidase activity in dairy products. Journal of Dairy Science 60 170–176CrossRefGoogle Scholar
Eriksson, C. E. 1970 Nonenzymatio lipid oxidation by lactoperoxidase. Effect of heat treatment. Journal of Dairy Science 53 1649–1653CrossRefGoogle Scholar
Eriksson, C. E., Olsson, P. A. & Svensson, S. G. 1971 Denatured hemoproteins as catalysts in lipid oxidation. Journal of the American Oil Chemists' Society 48 442–447CrossRefGoogle ScholarPubMed
Fridovich, S. E. & Porter, N. A. 1981 Oxidation of arachidonic acid in micelles by superoxide and hydrogen peroxide. Journal of Biological Chemistry 256 260–265CrossRefGoogle ScholarPubMed
Gordon, W. G., Ziegler, J. & Basch, J. J. 1962 Isolation of an iron-binding protein from cow's milk. Biochimica et Biophysica Acta 60 410–411CrossRefGoogle Scholar
Gregory, J. F., Babish, J. G. & Shipe, W. F. 1976 Role of heme proteins in peroxidation of milk lipids. Journal of Dairy Science 59 364–368CrossRefGoogle Scholar
Groves, M. L. 1960 The isolation of a red protein from milk. Journal of the American Chemical Society 82 3345–3350CrossRefGoogle Scholar
Groves, M. L. 1971 Minor milk proteins and enzymes. In Milk Proteins Vol. 2(Ed.McKenzie, H. A.)pp. 367–418. London: Academic PressCrossRefGoogle Scholar
Hasegawa, K. & Patterson, L. K. 1978 Pulse radiolysis studies in model lipid systems: formation and behaviour of peroxy radicals in fatty acids. Photochemistry and Photobiology 28 817–823CrossRefGoogle Scholar
Haurowitz, F., Groh, M. & Gansinger, G. 1973 Mechanism and kinetics of the hemin-catalyzed oxidation of linoleate in the oil-water interface. Journal of Biological Chemistry 248 3810–3818CrossRefGoogle ScholarPubMed
Hill, R. D. 1975 Superoxide dismutase activity in bovine milk Australian Journal of Dairy Technology 30 26–28Google Scholar
Hill, R. D. 1979 Oxidative enzymes and oxidative processes in milk. Commonwealth Scientific and Industrial Research Organisation, Food Research Quarterly 39 33–37Google Scholar
Hill, R. D., Van Leeuwen, V. & Wilkinson, R. A. 1977 Some factors influencing the autoxidation of milks rich in linoleic acid. New Zealand Journal of Dairy Science and Technology 12 69–77Google Scholar
Holbrook, J. & Hicks, C. L. 1978 Variation of superoxide dismutase in bovine milk. Journal of Dairy Science 61 1072–1077CrossRefGoogle Scholar
Kalckar, H. M. 1947 Differential spectrophotometry of purine compounds by means of specific enzymes. I. Determination of hydroxypurine compounds. Journal of Biological Chemistry 167 429–443CrossRefGoogle 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 8812–8817CrossRefGoogle Scholar
Labuza, T. P. 1971 Kinetics of lipid oxidation in foods. CRC Critical Reviews in Food Technology 2 355–405CrossRefGoogle Scholar
Law, B. A. & Reiter, B. 1977 The isolation and bacteriostatic properties of lactoferrin from bovine milk whey Journal of Dairy Research 44 595–599CrossRefGoogle ScholarPubMed
Lynch, R. E. & Fridovich, I. 1979 Autoinactivation of xanthine oxidase. The role of superoxide radical and hydrogen peroxide. Biochimica et Biophysica Acta 571 195–200CrossRefGoogle ScholarPubMed
Masson, P. L. & Heremans, J. F. 1968 Metal-combining properties of human lactoferrin (red milk protein). 1. The involvement of bicarbonate in the reaction. European Journal of Biochemistry 6 579–584CrossRefGoogle ScholarPubMed
McCord, J. M. & Fridovich, I. 1969 Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein). Journal of Biological Chemistry 244 6049–6055CrossRefGoogle ScholarPubMed
McMillan, J. A., Oski, F. A., Lourie, G., Tomarelli, R. M. & Landaw, S. A. 1977 Iron absorption from human milk, simulated human milk and proprietary formulas. Pediatrics USA 60 896–900CrossRefGoogle ScholarPubMed
Morrison, M. & Hultquist, D. E. 1963 Lactoperoxidase. II. Isolation. Journal of Biological Chemistry 238 2847–2849CrossRefGoogle ScholarPubMed
Polis, B. D. & Shmukler, H. W. 1953 Crystalline lactoperoxidase. I. Isolation by displacement chromato-graphy. II. Physiochemical and enzymatic properties. Journal of Biological Chemistry 201 475–500CrossRefGoogle Scholar
Samuelsson, E. G. 1966 The copper content in milk and the distribution of copper to some various phases of milk. Milchwissenschaft 21 335–341Google Scholar
Smith, G. J. & Dunkley, W. L. 1962 Copper binding in relation to inhibition of oxidized flavor by heat treatment and homogenization. 16th International Dairy Congress, Copenhagen A, 625–630Google Scholar
Tappel, A. L. 1955 Unsaturated lipid oxidation catalyzed by hematin compounds. Journal of Biological Chemistry 217 721–733CrossRefGoogle ScholarPubMed
Tappel, A. L. 1961 Lipoxidase and hematin biocatalysts. III. Catalysis of unsaturated lipid oxidation by hematin compounds. In Autoxidation and Antioxidants Vol. 1 (Ed. Lundberg, W. O.) pp. 346–366. New York: WileyGoogle Scholar
Thomas, M. J., Mehl, K. S. & Pryor, W. A. 1978 The role of the super-oxide anion in the xanthine oxidase-induced autoxidation of linoleic acid. Biochemical and Biophysical Research Communications 83 927–932CrossRefGoogle Scholar