Effect of Maillard Browning Reaction on Nutritional Quality of Protein

  • M. Tanaka
  • M. Kimiagar
  • Tung-Ching Lee
  • C. O. Chichester
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 86)


The Maillard reaction, or non-enzymatic browning reaction, between reducing sugars and proteins (amino acids), is known to cause serious deterioration of food quality during processing and storage. Increasing evidence shows that these compounds formed under mild conditions substantially reduce the availability of amino acids and proteins. Data obtained by ourselves and others has shown there is a significant decrease in the nutritional value of foods which undergo the Maillard reaction beyond that accounted for in the loss of biologically available lysine. In the present investigation, a mixture of egg albumin and glucose was used as a model system. The nutritional quality of egg albumin as a function of the extent of Maillard browning with periods of less than 10 days of storage was evaluated by in vivo and in vitro methods. A substantial decrease in nutritional quality of protein was observed even at the initial period of storage (less than three days) and most available in vitro methods could not reveal this change. The result of a three-month rat feeding experiment indicated that there were physiological and biochemical changes in rats fed with browned protein diet. It is extremely inportant at the present time to have information on the nutritional value and aspects of food safety of browned food products with respect to nutritional labelling policy. Therefore, in addition to the development of new food products with high protein quality, the practical applications of this study are also discussed.


Nutritional Quality Maillard Reaction Protein Quality Protein Efficiency Ratio Serum Glutamate Pyruvate Transaminase 
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  1. Adrian, J. 1974. Nutritional and physiological consequences of the Maillard reaction. World Rev. of Nutr. and Diet. 19: 71.Google Scholar
  2. Amaya, J. F. 1974. The Maillard reaction of proteins. Ph.D. disser- tation. University of Rhode Island, Kingston, R. I. 02881.Google Scholar
  3. Amaya, J. F., Tung-Ching Lee and C. 0. Chichester. 1976. Biological inactivation of proteins by the Maillard reaction. Effect of mild heat on the tertiary structure of insulin. J. Agric. Food Chem. 24: 465.Google Scholar
  4. Bjarnason, J. and K. J. Carpenter. 1969. Mechanisms of heat damage in proteins, I. Models with acylated lysine units. Brit. J. Nutr. 23: 859.Google Scholar
  5. Bjarnason, J. and K. J. Carpenter. 1970. Mechanisms of heat damage in proteins, II. Chemical changes in pure proteins. Brit. J. Nutr. 24: 313.Google Scholar
  6. Boctor, A. M. and A. E. Harper. 1968. Measurement of available lysine in heated and unheated foodstuffs by chemical and biological methods. J. Nutr. 94: 289.PubMedGoogle Scholar
  7. Boyd, W. 1965. Textbook of pathology. Seventh. edition. Lea and Febiger, Philadelphia, Pennsylvania. p. 552.Google Scholar
  8. Carpenter, K. J. 1960. The estimation of available lysine in animal protein foods. Biochem. J. 77: 604.Google Scholar
  9. Carpenter, K. J. and V. H. Booth. 1973. Damage to lysine in food processing: Its measurement and significance. Nutr. Abs. Rev. 43: 424.Google Scholar
  10. Chichester, C. O. 1973. Nutrition in food processing. World Rev. Nutr. and Diet. 16: 318.Google Scholar
  11. Chinsky, M., G. L. Shmagranoff and S. Sherry. 1956. Serum transaminase activity. J. Lab. and Clin. Med. 47: 108.Google Scholar
  12. Clinger, C., A. Yound, I. Prudent and A. R. Winter. 1951. The influence of pasteurization, freezing and storage on the functional properties of egg white. Food Technol. 5: 166.Google Scholar
  13. Coduri, R. J. and A. G. Rand, Jr. 1972. Vertical plate gel electrophoresis for the differentiation of meat species. J. A. O. A. C. 55: 461.Google Scholar
  14. Dahlquist, A. 1964. Method for assay of intestinal disaccharidases. Anal. Biochem. 7: 18.Google Scholar
  15. Erbersdobler, H. 1969. AminosHurenanflutung im pfortaderplasma nach fiítterung hitzegeschHdigten proteins und hocheiweissadaptierter ratten. Z. Tierphysiol. TierernHhr. Futtermittelk. 25: 119.Google Scholar
  16. Fink, H., I. Schlie and U. Ruge. 1958. Über ernHhrung-sphysiologi- sche verdnderungen der milch beim technischen trocknen. Z. Naturforsch. 13B: 610.Google Scholar
  17. Ford, J. E. and C. Shorrock. 1971. Influence of heat damaged proteins in the rat. Brit. J. Nutr. 26: 311.Google Scholar
  18. Henry, K. M., S. K. Kon, C. H. Lea and J. C. D. White. 1948. Deterioration on storage of dried milk. J. Dairy Res. 15: 292.CrossRefGoogle Scholar
  19. Josefsson, L. and T. Lindberg. 1965. Intestinal dipeptidases. Biochem. Biophys. Acta. 105: 149.Google Scholar
  20. Kakade, M. L. and I. E. Liener. 1969. Determination of available lysine in proteins. Anal. Biochem. 27: 273.Google Scholar
  21. Karmen, A., F. Wroblewski and J. S. LaDue. 1955. Transaminase activity in human blood serum. J. Clin. Invest. 34: 126.Google Scholar
  22. Lee, C. M. 1974. Physiological consequences of non-enzymatic browning. Ph.D. dissertation. University of Rhode Island, Kingston, Rhode Island 02881.Google Scholar
  23. Lee, C. M., Tung-Ching Lee and C. 0. Chichester. 1976. Physiological consequences of browned food products. Proceedings of the IV International Congress of Food Science and Technology (in press).Google Scholar
  24. Lowry, O. H., N. J. Rosebrough, A. L. Parr and R. J. Randall. 1951. Protein measurement with the folin phenol reagent. J. Biol. Chem. 193: 265.Google Scholar
  25. Mauron, J., F. Mottu, E. Bujard and R. H. Egli. 1955. The availability of lysine, methionine and tryptophan in condensed milk and milk powder “in vivo” digestion studies. Arch. Biochem. Biophys. 59: 433.Google Scholar
  26. Nesheim, M. C. and K. J. Carpenter. 1967. The digestion of heat-damaged protein. Brit. J. Nutr. 21: 399.Google Scholar
  27. Newmann, H. and M. Van Vreedendaal. 1967. An improved alkaline phosphatase determination with p-nitrophenyl phosphate. Clin. Chim. Acta. 17: 183.Google Scholar
  28. Patton, S. 1955. Browning and associated changes in milk and its products. A review. J. Dairy Sci. 38: 457.Google Scholar
  29. Rand, N. T., V. K. Collins, D. S. Varner and J. D. Masser. 1960. Biological evaluation of the factors affecting the protein quality of fish meals. Poultry(Sci. 39: 45.CrossRefGoogle Scholar
  30. Root, H. F. and C. C. Bailey. 1964. In: Modern Nutrition in Health and Disease. Ed. by Whol and Goodhart. Lee and Febiger, Philadelphia, Pennsylvania. p. 796.Google Scholar
  31. Sauberlich, H. E. 1961. Growth of rats fed protein-free diets supplemented with purified amino acid mixtures. J. Nutr. 74: 298.Google Scholar
  32. Sgarbieri, V. C., M. Tanaka, C. O. Chichester and J. Amaya. 1971.Google Scholar
  33. Some nutritional consequences of the Maillard reaction. Proceedings of III Western Hemisphere Nutrition Congress. Futura Publishing Co., Mount Kisco, New York. p. 330.Google Scholar
  34. Sigma Chemical Company Technical Bulletin. 1975. No. 535. The colorimetric determination of urea nitrogen in blood, plasma or serum. Sigma Chemical Company, St. Louis, Missouri.Google Scholar
  35. Tanaka, M. 1974. Effect of the browning reaction on quality, digestion and absorption of protein. Ph.D. dissertation. University of Rhode Island, Kingston, Rhode Island 02881Google Scholar
  36. Tanaka, M., J. Amaya, Tung-Ching Lee and C. O. Chichester. 1976. Proceedings of the IV International Congress of Food Science and Technology (in press).Google Scholar
  37. Tanaka, M., Tung-Ching Lee and C. O. Chichester. 1975. Nutritional consequences of the Maillard reaction. The absorption of fructose-L-tryptophan in the large intestine of the rat. J. Nutr. 105: 989.Google Scholar
  38. Tanaka, M., Tung-Ching Lee and C. O. Chichester. 1975. Effect of browning on chemical properties of egg albumin. Agric. Biol. Chem. 39: 863.Google Scholar

Copyright information

© Springer Science+Business Media New York 1977

Authors and Affiliations

  • M. Tanaka
    • 1
  • M. Kimiagar
    • 1
  • Tung-Ching Lee
    • 1
  • C. O. Chichester
    • 1
  1. 1.Department of Food Science and TechnologyUniversity of Rhode IslandKingstonUSA

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