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Reactions of proteins with oxidizing lipids

2. Influence on protein quality and on the bioavailability of lysine, methionine, cyst(e)ine and tryptophan as measured in rat assays

Published online by Cambridge University Press:  07 March 2008

Henrik K. Nielsen ,
P. A. Finot  and
R. F. Hurrell
Henrik K. Nielsen
Affiliation:
Research Department, NestIé Products Technical Assistance Co. Ltd, CH-1814 La Tour-de-Peilz, Switzerland
P. A. Finot
Affiliation:
Research Department, NestIé Products Technical Assistance Co. Ltd, CH-1814 La Tour-de-Peilz, Switzerland
R. F. Hurrell
Affiliation:
Research Department, NestIé Products Technical Assistance Co. Ltd, CH-1814 La Tour-de-Peilz, Switzerland
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Abstract

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1. The consequences of reactions between protein and oxidizing lipids on the nutritional quality of food proteins have been investigated using a whey protein–methyl linolenate-water model system.

2. In rat assays, significant reductions were observed in protein efficiency ratio, net protein ratio, net protein utilization, biological value and true nitrogen digestibility, especially when the reaction had taken place at high moisture content, high temperature and in the presence of excess oxygen.

3. The losses of bioavailable lysine and tryptophan as measured by rat assays followed a similar pattern. The chemical value of each amino acid multiplied by the true N digestibility closely resembled the rat assay value. In general, the reaction products of lysine and tryptophan formed during lipid oxidation were biologically unavailable.

4. The bioavailabilities of methionine and of ‘methionine plus cyst(e)ine’ were determined in separate assays. Cyst(e)ine was calculated as ‘methionine plus cyst(e)ine’ minus methionine. In whey protein which had reacted with oxidizing methyl linolenate, the bioavailable methionine content was not significantly reduced even though 82% of the methionine residues were present as methionine sulphoxide. In hydrogen peroxide-treated casein in which all methionine residues were oxidized to the sulphoxide, methionine sulphoxide was found to be 96% as utilizable as a methionine source to the rat. Free methionine sulphoxide was 87% utilizable.

5. Cyst(e)ine appeared to be as sensitive as lysine to reactions with lipid oxidation products. In whey protein which had reacted with oxidizing methyl linolenate, the bioavailabilities of cyst(e)ine, lysine, tryptophan and methionine were reduced by 28, 24, 11 and 8% respectively and true N digestibility by 9%. These results are discussed in relation to food products.

Type
Papers on General Nutrition
Information
British Journal of Nutrition , Volume 53 , Issue 1 , January 1985 , pp. 75 - 86
Copyright
Copyright © The Nutrition Society 1985

References

REFERENCES

Anderson, G. H., Ashley, D. M. V. & Jones, J. F. (1976). Journal of Nutrition 106, 1108–1114.CrossRefGoogle Scholar
Association of Official Analytical Chemists (1980). Official Methods of Analysis of the Association of Official Analytical Chemists, p. 774 [Horwitz, W., editor]. Washington DC: AOAC.Google Scholar
Bender, A. E. & Doell, B. H. (1957). British Journal of Nutrition 11, 140–148.CrossRefGoogle Scholar
Bennett, M. A. (1937). Biochemical Journal 31, 962–965.CrossRefGoogle Scholar
Bennett, M. A. (1939). Biochemical Journal 33, 885–892.CrossRefGoogle Scholar
Byington, M. H., Howe, J. M. & Clark, H. E. (1972). Journal of Nutrition 102, 219–228.CrossRefGoogle Scholar
Cuq, J.-L., Besancon, P., Chartier, L. & Cheftel, C. (1978). Food Chemistry 3, 85–101.CrossRefGoogle Scholar
Finkelstein, J. D. & Mudd, S. H. (1967). Journal of Biological Chemistry 242, 873–880.CrossRefGoogle Scholar
Finley, J. W., Wheeler, E. L. & Witt, S. C. (1981). Journal of Agricultura1 and Food Chemistry 29, 404–407.CrossRefGoogle Scholar
Finney, D. J. (1964). Statistical Methods in Biological Assay, 2nd ed.New York: Hafner Publishing Co.Google Scholar
Food and Agriculture Organization (1970). Amino-acid Content of Foods and Biological Data on Proteins. Rome: FAOGoogle Scholar
Gamage, P. T. & Matsushita, S. (1973). Agricultural and Biological Chemistry 37, 1–8.Google Scholar
Gjöen, A. V. & Njaa, L. R. (1977). British Journal of Nutrition 37, 93–105.CrossRefGoogle Scholar
Harmuth-Hoene, A. E. & Delincée, H. (1978). International Journal for Vitamin and Nutrition Research 48, 62–74.Google Scholar
Horigome, T. & Miura, M. (1974). Journal of the Agricultural Chemistry Society of Japan 48, 437–444.Google Scholar
Horigome, T. & Uchida, S. (1979). Scientific Reports of the Faculty of Agriculture, Okayama University 54, 43–49.Google Scholar
Horigome, T., Yanagida, T. & Miura, M. (1974). Journal of the Agricultural Chemistry Society of Japan 48, 195–199.Google Scholar
Hurrell, R. F. (1980). In Food and Health – Science and Technology, pp. 369–388 [Birch, G. G. and Parker, K. J., editors]. London: Applied Science Publishers.CrossRefGoogle Scholar
Hurrell, R. F. (1984). In Food Proteins, vol. 3 [Hudson, B. J. F., editor]. London: Applied Science Publishers.Google Scholar
James, K. A. C. & Hove, E. L. (1980). Journal of Nutrition 110, 1736–1744.CrossRefGoogle Scholar
Kanazawa, K., Danno, G. & Natake, M. (1975). Journal of Nutritional Science and Vitaminology 21, 373–382.CrossRefGoogle Scholar
Marable, N. L., Todd, J. M., Korslund, M. K. & Kennedy, B. W. (1980). Qualitas Plantarum – Plant Foods for Human Nutrition 30, 155–161.CrossRefGoogle Scholar
Mitchell, H. H. (1923–24). Journal of Biological Chemistry 58, 873–905.CrossRefGoogle Scholar
Mottu, F. & Mauron, J. (1967). Journal of the Science of Food and Agriculture 18, 57–62.CrossRefGoogle Scholar
Nielsen, H. K., De Weck, D., Finot, P. A., Liardon, R. & Hurrell, R. F. (1985 a). British Journal of Nutrition 53 (In the Press.)Google Scholar
Nielsen, H. K., Löliger, J. & Hurrell, R. F. (1985 b). British Journal of Nutrition 53, 61–73.CrossRefGoogle Scholar
Njaa, L. R. (1962). British Journal of Nutrition 48, 565–570.CrossRefGoogle Scholar
O'Brien, P. J. (1966). Biochemical Journal 101, 12P–13P.Google Scholar
Pellet, P. L. & Young, V. R. (1980). Nutritional Evaluation of Protein Foods. United Nations University: Tokyo.Google Scholar
Peret, J., Macaire, F. & Chanez, M. (1973). Journal of Nutrition 103, 866–874.CrossRefGoogle Scholar
Rogers, Q. R. & Harper, A. E. (1965). Journal of Nutrition 87, 267–273.CrossRefGoogle Scholar
Sjöberg, L. B. & Boström, S. L. (1977). British Journal of Nutrition 38, 189–205.CrossRefGoogle Scholar
Slump, P. & Schreuder, H. A. W. (1973). Journal of the Science of Food and Agriculture 24, 657–661.CrossRefGoogle Scholar
Stockland, W. L., Meade, R. J., Wass, D. F. & Sowers, J. E. (1973). Journal of Animal Science 36, 52&530.CrossRefGoogle Scholar
Yanagita, T. & Sugano, M. (1973). Journal of the Agricultural Chemistry Society of Japan 47, 577–582.Google Scholar
Yanagita, T. & Sugano, M. (1975). Agricultural and Biological Chemistry 39, 63–69.Google Scholar
Yanagita, T. & Sugano, M. (1978). Journal of Nutritional Science and Vitaminology 24, 581–588.CrossRefGoogle Scholar