Abstract
To assess whether the dipeptide N-ε-(γ-L-glutamyl)-L-lyslne (glutamyl-lysine) can serve as a nutritional source of lysine, we compared the growth of mice fed (a) an amino acid diet in which lysine was replaced by six dietary levels of glutamyl-lysine; (b) wheat gluten diets fortified with lysine; (c) a wheat bread-based diet (10% protein) supplemented before feeding with lysine or glutamyl-lysine (0, 0.75, 1.50, 2.25, and 3% lysine HCl-equivalent in the final diet), not co-baked and (d) bread diets co-baked with these levels of lysine or glutamyl-lysine. With the amino acid diet, the relative growth response to glutamyl-lysine was about half that of lysine. The effect of added lysine on the nutritional improvement of wheat gluten depended on both lysine and gluten concentrations in the diet. With 10 and 15% gluten, 0.37% lysine HC1 produced a marked increase in weight gain. Further increase in lysine HC1 to 0.75% proved deterimental to weight gain. Lysine HC1 addition improved growth at 20 and 25% gluten in the diet and did not prove detrimental at 0.75%. For whole bread, glutamyl-lysine served nearly as well as lysine to improve weight gain. The nutritive value of bread crust fortified or not was markedly less than that of crumb or whole bread. Other data showed that lysine or glutamyl-lysine at the highest level of fortification, 0.3%, improved the protein quality (PER) of crumb over that of either crust or whole bread, indicating a possible greater availability of the second-limiting amino acid, threonine, in crumb. These data and additional metabolic studies with U-14 -C glutamyl-lysine suggest that glutamyl-lysine, co-baked or not, is digested in the kidneys and utilized in vivo as a source of lysine; it and related peptides merit further study as a sources of lysine in low-lysine foods.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Bell, J.M., and John, A.M. Amino acid requiremnts of growing mice: arginine, lysine, tryptophan and phenylalanine. J. Nutr., 111, 525–530. 1981.
Betschart, A.A. Improving protein quality of bread-nutritional benefits and realities. In “Nutritional Improvement of Food and Feed Proteins-Adv. Exp. Med. Biol. 105”, M. Friedman, Ed., Plenum, New York, pp 703–734. 1978.
Bjorck, I., Noguchi, A., Asp, N.G., Cheftel, J., and Dahlqvist, A. Protein nutritional value of a biscuit processed by extrusion cooking: effects on available lysine. J. Agric. Food Chem., 31, 488–492. 1983.
Cavins, J.F., and Friedman, M. New amino acids derived from reactions of ε-amino groups in proteins with α, β-unsaturated compounds. Biochemistry 6, 3766–3770. 1967.
Cavins, J.F., and Friedman, M. Automatic integration and computation of amino acid analyses. Cereal Chem. 45, 172–176. 1968.
Chan, E.L., and Nakai, S. Comparison of browning in wheat glutens enriched by covalent attachment and addition of lysine. J. Agric. Food Chem., 29, 1200–1205. 1981.
Chan, E.L., Helbig, N., Holbek, E., Chan, S., and Nakai, S. Covalent attachment of lysine to wheat gluten for nutritional improvement. J. Agic. Food Chem., 27, 877–882. 1979.
Chu, S.H., and Hegsted, D.M. Adaptive response of lysine and threonine degrading enoymes in adult rats. J. Nutr., 106, 1089–1096. 1976.
Cossack, Z.T., and Weber, C.W. A proposed bioassay for evaluating protein quality using rats and mice. Nutr. Rep. Int., 28, 203–218. 1983
De Weck-Gaudard, D., Liardon, R., and Finot, P.A. Stereomeric composition of urinary lysinoalanine after ingestion of free or protein-bound lysinoalanine in rats. J. Agric. Food Chem., 36, 721–725. 1988.
Eskins, K., and Friedman, M. Solvent effects during the photochemistry of gluten-proteins. Photochem. Photobiol. 12, 245–247. 1970a.
Eskins, K., and Friedman, M. Graft photopolymerization of styrene to wheat gluten proteins in dimethyl sulfoxide. J. Macromol. Sci. A4, 947–956. 1970b.
Finley, J.W. and Friedman, M. Chemical methods for available lysine. Cereal Chemistry 50, 101–105. 1973.
Fink, M.L., Chung, S.I., and Folk, J.E. γ-Giutamylamine cyclotransferase: specificity toward ε-(L-γ-glutamyl)-L-1ysine and related compounds. Proc. Natl. Acad Sci. USA. 77, 4564–4568. 1980.
Finney, D.J. Statistical Methods in Biological Assay. 3rd Ed., McMillan: New York, p 508. 1978.
Finot, P.A., Mottu, F., Bujard, E., and Mauron, J. N-substituted lysines as a source of lysine in nutrition. In “Nutritional Improvement of Food and Feed Proteins”, M. Friedman, Ed., Plenum, New York, pp 549–569. 1978.
Friedman, M. Reactions of cereal proteins with vinyl compound. In “Industrial Uses of Cereal Grains”, Y. Pomeranz, Editor, American Association of Cereal Chemists, Minneapolis, MN, PP. 237–251. 1973.
Friedman, M. (Editor). “Protein Nutritional Quality of Foods and Feeds”, Marcel Dekker, New York. 2 Volumes. 1975.
Friedman, M. Effect of lysine modification on chemical, physical, nutritive, and functional properties of proteins. In “Food Proteins”, J.R. Whitaker and S. Tannenbaum, Eds., Avi, Westport, CT, pp. 446–483. 1977a.
Friedman, M. Crosslinking amino acids-stereochemistry and nomenclature. In “Protein Crosslinklng: Nutritional and Medical Consequences”-Adv. Exp. Med. Biol. 86B, M. Friedman, Ed., Plenum, New York, pp. 1–27. 1977b.
Friedman, M. (Editor). “Protein Crosslinklng: Nutritional and Medical Consequences”, Plenum Press, New York, 1977c.
Friedman, M. (Editor). “Protein Crosslinking: Biochemical and Molecular Aspects”, Plenum Press, New York, 1977d.
Friedman, M. Wheat gluten-alkali reactions. In “Proceedings of the 10th National Conference on Wheat Utilization Research”, U.S. Department of Agriculture, Science and Education Administration, Western Regional Research Center, Berkeley, CA, ARM-W-4, pp. 81–100. 1978a.
Friedman, M. (Editor). “Nutritional Improvement of Food and Feed Proteins”, Plenum Press, New York, 1978b.
Friedman, M. Alkali-induced lysinoalanine formation in structurally different proteins. In “Protein Structure Related to Functionality”, A-Pour-El, Ed., ACS Symposium Series, Washington, D.C. 92, 225–235. 1979.
Friedman, M. Chemically reactive and unreactive lysine as an index of browning. Diabetes, 31(3), 5–14. 1982.
Friedman, M. (Editor). “Absorption and Utilization of Amino Acids”, CRC Press, Boca Raton, Florida. 3 Volumes. 1989.
Friedman, M., and Finley, J. W. Vinyl compounds as reagents for determining available lysine in proteins. In “Protein Nutritional Quality of Foods and Feeds”, Marcel Dekker, New York, Part 1, pp. 503–520. 1975.
Friedman, M., and Gumbmann, M.R. Bloavallability of some lysine derivatives in mice. J. Nutr., 111, 1362–1369. 1981.
Friedman, M., and Gumbmann, M.R. Nutritional value and safety of methionine derivatives, isomeric dipeptides and hydroxy analogs in mice. J. Nutr., 118. 388–397. 1988.
Friedman, M., Krull, L.H., and Cavins, J.F. The Chromatographic determination of cysteine and half-cystine residues in proteins as S-ß-(4-pyridylethyl)-L-cysteine. J. Biol. Chem. 245, 3868–3871. 1970.
Friedman, M., Noma, A.T., and Wagner, J.R. Ion-exchange chromatography of sulfur amino acids on a single-column amino acid analyzer. Anal. Biochem., 98, 293–304. 1979.
Friedman, M., Gumbmann, M.R., and Savoie, L. The nutritional value of lysinoaianine as a source of lysine for mice. Nutr. Rep. Int., 26, 939–947. 1982.
Friedman, M., Gumbmann, M.R., and Masters, P.M. Protein-alkali reactions: chemistry, toxicology, and nutritional consequences. In “Nutritional and Toxicological Aspects of Food Safety-Adv. Exp. Med. Biol. 177”, M. Friedman, Ed., Plenum, New York, pp. 367–412. 1984a.
Friedman, M., Pang, J., and Smith, G.A. Ninhydrin-reactive lysine in food proteins. J. Food Sci. 49, 10–13. 1984b
Friedman, M., Gumbmann, M.R., and Ziderman, I.I. Nutritional value and safety in mice of proteins and their admixtures with carbohydrates and vitamin C. J. Nutr., 117. 508–518. 1987.
Friedman, M., Gumbmann, M.R., and Brandon, D.L. Nutritonal, toxicological, and immunological consequences of food processing. Frontiers Gastsrointestinal Research 14, 79–90. 1988.
Friedman, M., Wilson, R.W., and Ziderman, I.I. Mutagen formation in heated wheat gluten, carbohydrates, and gluten/carbohydrate blends. J. Agric. Food Chem., 38. 1019–1028. 1990.
Geervani, P., and Devi, P.Y. Effect of different heat treatments on losses of lysine in processed products prepared from unfortified flour and flour fortified with lysine. Nutr. Rep. Int., 33, 961–966. 1986.
Gumbmann, M.R., Friedman, M., and Smith, G.A. The nutritional values and digestibilities of heat damaged casein and casein-carbohydrate mixtures. Nutr. Rep. Int., 28, 355–361. 1983.
Hegsted, D.M. Protein quality and its determination. In “Food Proteins”, J.R. Whitaker, S.R. Tannenbaum, Eds., AVI, Westport, CT, pp. 347–362. 1977.
Hurrell, R.R., and Carpenter, K.J. Nutritional significance of cross-link formation during food processing. Adv. Exp. Med. Biol., 86B, 225–237. 1977.
Ikura, K., Okumura, K., Yoshikawa, M., Sasaki, R., and Chiba, H. Incorporation of lysyldipeptides into food protein by transglutaminase. Agric. Biol. Chem., 49, 1877–1878. 1985.
Iwami, K., and Yasucnoto, K. Amine-binding capacities of food proteins in transgiutaminase reaction and digestibility of wheat gliadin with c-attached lysine. J. Sci. Food Agric. 37, 495–503. 1986.
Jansen, R.G. Amino acid fortification. In “New Protein Foods”, A.M. Altschul and H.L. Wilcke, Eds., Academic Press, New York, Vo. 4, pp. 161–204. 1981.
Johnson, V.A., and Mattern, P.J. Improvement of wheat protein quality and uantity by breeding. In “Nutritional Improvement of Food and Feed Proteins-Adv. Exp. Med. Biol. 105” M. Friedman, Ed., Plenum, New York, pp. 301–316. 1978.
Khan-Siddiqui, K. Lysine-carnitine conversion in rat and man. In “Absorption and Utilization of Amino Acids”, M. Friedman, Ed., CRC, Boca Raton, FL, Vol. 2, pp 41–57. 1989.
Kritchevsky, D.A. Dietary protein in atherosclerosis. In “Absorption and Utilization of Amino Acids”, M. Friedman, Ed., CRC, Boca Raton, FL, Vol. 2, pp 235–245. 1989.
Krull, L.H., and Friedman, M. Anionic polymerization of methyl acrylate to protein functional groups. J. Polym. Sci. A-1, 5, 2535–2546. 1967.
Kurth, L., and Rogers, P.J. Transglutaminase catalyzed cross-linking of myosin to soya protein, casein and gluten. J. Food Sci., 49, 573–576. 1984.
Liardon, R., Friedman, M., and Phillippossian, G. Racemization kinetics of free-and protein-bound lysinoalanine (LAL) in strong acid media. Isomeric composition of protein-bound LAL. J. Agric. Food Chem. 38, 1990, submitted.
Loewy, A.G. The N-ε-(γ-glutamic) lysine cross-link: method of analysis, occurrence in extracellular and cellular proteins. Methods Enzvmol., 107. 241–257. 1984.
Lougnon, L., and Kiener, T. Biological utilization of basic amino acids and cations. In “Absorption and Utilization of Amino Acids”, M. Friedman, Ed., CRC, Boca Raton, FL, Vol. 2, pp 1–24. 1989.
Menefee, M., and Friedman, M. Estimation of structural components of abnormal hair from amino acid analyses. J. Protein Chem. 4, 333–341. 1985.
Milner, J.A. Arginine: a dietary modifier of ammonia detoxification and pyrimidine biosynthesis. In “Absorption and Utilization of Amino Acids”, M. Friedman, Ed., CRC, Boca Raton, FL, Vol. 2, pp. 26–40. 1989.
Motoki, M., and Nio, N. Crosslinking between different food proteins by transglutaminase. J. Food Sci., 48, 561–566. 1983.
Otterburn, M.S. Protein crosslinking. In “Protein Quality and the Effects of Processing”, R.D. Phillips, J.W. Finley, Eds., Marcel Oekker, New York, pp. 247–261. 1989.
Otterburn, M., Healy, M., and Sinclair, W. The formation, isolation, and maintenance and growth. In “Absorption and Utilization of Amino Acids”, M. Friedman, Ed., CRC, Boca Raton, FL., Vol. 1, pp. 15–30. 1989.
Owens, F.N., and Pettigrew, O.E. Subdividing amino acid requirements for maintenance and growth. In “Absorption and Utilization of Amino Acids”, M. Friedman, Ed., CRC, Boca Raton, FL., Vol 1, pp. 15–30. 1989.
Pearce, K.N., Karahalios, D., and Friedman, M. Ninhydrin assay for proteolysis in ripening cheese. J. Food Sci. 52, 432–435. 1988.
Raczynski, G., Snochowski, M., and Buraczewski, S. Metabolism of ε-(γ-L-glutamyl)-L-lysine in the rat. Br. J. Nutr., 34. 291–296. 1975.
Reichl, J.R. Absorption and metabolism of amino acids studies in vitro, in. vivo, and with computer simulations. In “Absorption and Utilization of Amino Acids”, M. Friedman, Ed., CRC, Boca Raton, FL., Vol. 1, pp. 93–156. 1989.
Sanchez, A., and Hubbard, R.W. Dietary protein modulation and serum cholesterol: the amino acid connection. In “Absorption and Utilization of Amino Acids”, M. Friedman, Ed., CRC, Boca Raton, FL, Vol. 2, pp. 247–273. 1989
Sarwar, G., and Paquet, A. Availability of amino acids in some tripeptides and derivatives present in dietary proteins. In “Absorption and Utilization of Amino Acids”, M. Friedman, CRC, Boca Raton, FL, Volume 2, pp. 147–154. 1989.
Sarwar, G., Christensen, D. A., Finlayson, A. J., Friedman, M., Hackler, L. R., Mackenzie, S. L., Pellet, P. L., and Tkachuk, R. Intra-and inter-laboratory variation in amino acid analysis. J. Food Sci., 48. 526–531. 1983.
Sarwar, G., Blair, R., Friedman, M., Gumbmann, M. R., Hackler, L. R., Pelletl, P. L., and Smith, T. L. Inter-and intra laboratory variability in rat growth assays for estimating protein quality in foods. J. Assoc. Off. Anal. Chem. 67, 976–981. 1984.
Sarwar, G., Blair, R., Friedman, M., Gumbmann, M. R., Hackler, L. R., Pellett, P. L., and Smith, T. K. Comparison of interlaboratory variation in amino acid analysis and rat growth assays for evaluating protein quality. J. Assoc. Off. Anal. Chem., 68, 52–56. 1985.
SAS. SAS/STAT Guide for Personal Computers; 6th Edition, SAS Institute: Cary, NC, 1028 p. 1987.
Scharrer, E. Regulation of intestinal amino acid transport. In “Absorption and Utilization of Amino Acids”, M. Friedman, Ed., CRC, Boca Raton, FL, Volume 1, pp. 57–68. 1989.
Sherr, B., Lee, C. M., and Jelesciewicz, C. Absorption and metabolism of lysine Maillard products in relation to the utilization of L-lysine. J. Agric. Food Chem., 37. 119–122 1989.
Tsen, C.C., and Reddy, P.R.K. Effect of toasting on the nutritive value of bread. J. Food Sci., 42. 1370–1372. 1977.
Tsen, C.C., Reddy, P.R.K., and Gehrke, C.W. Effects of conventional baking, microwave baking, and steaming on the nutritive value of regular and fortified breads. J. Food Sci., 42, 402–406. 1977.
Waibel, P.E., and Carpenter, K.J. Mechanism of heat damage in protein. 3. Studies with ε-(γ-L-glutamyl)-L-1ysine. Br. J. Nutr., 27, 509–515. 1972.
Zerbe, G. On Fieller’s theorem and General Linear Model. Am. Stat., 32, 103–105 1978.
Ziderman, I.I., and Friedman, M. Thermal and compositional changes of dry wheat gluten-carbohydrate mixtures during simulated crust baking. J. Agric. Food Chem., 33, 1096–1102. 1985.
Ziderman, I. I., Gregorski, K. S., and Friedman, M. Thermal analysis of protein-carbohydrate mixtures in oxygen. Thermochic.) Acta. 114, 109–114. 1987.
Ziderman, I.I., Gregorski, K.S., Lopez, S.V., and Friedman, M. Thermal interaction of ascorbic acid and sodium ascorbate with proteins in relation to nonenzymatic browning and Maillard reactions in foods. J. Agric. Food Chem. 37, 1480–1486. 1989.
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1991 Springer Science+Business Media New York
About this chapter
Cite this chapter
Friedman, M., Finot, PA. (1991). Improvement in the Nutritional Quality of Bread. In: Friedman, M. (eds) Nutritional and Toxicological Consequences of Food Processing. Advances in Experimental Medicine and Biology, vol 289. Springer, Boston, MA. https://doi.org/10.1007/978-1-4899-2626-5_30
Download citation
DOI: https://doi.org/10.1007/978-1-4899-2626-5_30
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4899-2628-9
Online ISBN: 978-1-4899-2626-5
eBook Packages: Springer Book Archive