Abstract
Treating wheat gluten, soy protein, and lactalbumin under alkaline conditions at 65°C for various times destroys part of the threonine, cystine, lysine, tyrosine, and arginine residues in these proteins. The losses were accompanied by the appearance of lysinoalanine and unidentified ninhydrin-positive substances. Treating wool under samewhat milder alkaline conditions destroys part of the cystine and lysine residues, but not the other amino acids cited. In this case, loss of cystine and lysine was accompanied by the appearance of lanthionine and lysinoalanine. Amino acid analysis of alkali-treated acylated proteins revealed that acylation by acetic and succinic anhydrides prevents or minimizes destruction of lysine residues and the formation of lysinoalanine in wheat gluten and soy protein and, in wool, minimizes destruction of cystine and lysine residues and the formation of lanthionine lysinoalanine. Mechanisms are proposed to explain the observed inhibiting effects of protein acylation and certain additives on lysinoalanine formation.
This is a preview of subscription content, log in via an institution to check access.
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
Cavins, J. F., and Friedman, M. (1968a). Automatic integration and computation of amino acid analyses. Cereal Chem., 45, 172–176.
Cavins, J. F., and Friedman, M. (1968b). Specific modification of protein sulfhydryl groups with a,6 -unsaturated compounds. J. Biol. Chem. 243: 3357–3360.
Cavins, J. F. and Friedman, M. (1967). New amino acids derived from reaction of c -amino groups in proteins with a,R -unsaturated compounds. Biochemistry, 6, 3766–3770.
Eskins, K., and Friedman, M. (1970a). Graft photopolymerization of styrene to wheat gluten proteins in dimethyl sulfoxide. J. Macromol. Sci. A4, 947–956.
Eskins, K., and Friedman, M. (1970b). Photoaddition of dimethyl sulfoxide to polypeptides. Photochem. Photobiol. 12, 245–247.
Eskins, K., Dintzis, F., and Friedman, M. (1971). Photopolymerization of methyl acrylate in dimethyl sulfoxide. J. Macromol. Sci. A5 (3) 543–548.
Farquharson, J. and Adams, J. F. (1977). Conversion of hydroxo (aquo)- cobalamin to sulfitocobalamin in the absence of light: a reaction of importance in the identification of the forms of vitamin B12, with possible clinical significance. Am. J. Clin. Nutri., 30, 1617–1622.
Finley, J. W. and Friedman, M. (1977). New amino acid derivatives formed by alkaline treatment of proteins. In “Protein Crosslinking: Nutritional and Medical Consequences,” M. Friedman, Ed., Plenum Press, New York, pp. 123–130.
Finley, J. W., Snow, J. T., Johnston, P. H., and Friedman, M. (1977). Inhibitory effect of mercaptoamino acids on lysinoalanine formation during alkali treatment of proteins. In “Protein Crosslinking: Nutritional and Medical Consequences,” M. Friedman, Ed., Plenum Press, New York, pp. 85–92.
Finot, P. A., Bujard, E., and Arnaud, M. (1977). Metabolfç transit of lysinoalanine bound to protein and free radioactive C- lysinoalanine. In “Protein Crosslinking: Nutritional and Medical Consequences”, M. Friedman, Ed., Plenum Press, New York, pp. 5171.
Friedman, M. (1977a). Crosslinking amino acids — stereochemistry and nomenclature. In “Protein Crosslinking: Nutritional and Medical Consequences,” M. Friedman, Ed., Plenum Press, New York, pp. 1–27.
Friedman, M. (1977b). Effects of lysine modification on chemical, physical, nutritive, and functional properties of proteins. In “Food Proteins”, J. R. Whitaker and S. R. Tannenbaum, Eds., Avi, Westport, Connecticut, pp. 446–483.
Friedman, M. (1973). Reactions of cereal proteins with vinyl compounds. In “Industrial Uses of Cereal Grains”, Y. Paneranz, Ed., American Association of Cereal Chemists, Minneapolis, Minnesota, pp. 237–251.
Friedman, M., and Broderick, G. A. (1977). Protected proteins in ruminant nutrition. In vitro evaluation of casein derivatives. In “Protein Crosslinking: Nutritional and Mbdical Consequences”, M. Friedman, Ed., Plenum Press, New York, pp. 545–558.
Friedman, M., Krull, L. H. (1969). A novel spectrophotometric procedure for the determination of half-cystine residues in proteins. Biochem. Biophys. Res. Commun. 37, 630–633.
Friedman, M. and Wall, J. S. (1964). Application of a Hammett-Taft relation to kinetics of alkylation of amino acids and peptide model compounds with acrylonitrile. J. Am. Chem. Soc., 86, 3735–3741.
Friedman, M., and Williams, L. D. (1973). The reaction of ninhy- drin with keratin proteins. Analyt. Biochem. 54, 333–345.
Friedman, M., and Williams, L. D. (1974). Stoichiometry of formation of Ruhemann’s purple in the ninhydrin reaction. Bioorganic Chemistry, 3, 267–280.
Friedman, M., Finley, J. W. and Yeh, Lai-Sue. (1977). Reactions of proteins with dehydrolanines. In “Protein Crosslinking: Nutritional and Medical Consequences”, M. Friedman, Ed., Plenum Press, New York, pp. 213–224.
Gee, M., Huxsoll, C. C., and Graham, R. P. (1974). Acidification of dry caustic peeling was by lactic acid fermentation. American Potato J., 51, 126–131.
Goldblatt, L. A. (1969). “Aflatoxin; Scientific Background, Control, and Implications”, Academic Press, New York.
Gould, D. H., and MacGregor, J. T. (1977). Biological effects of alkali-treated protein and lysinoalanine: an overview. In “Protein Crosslinking: Nutritional and Medical Consequences”, M. Friedman, Ed., Plenum Press, New York, pp. 29–48.
Habeeb, A. F. S. A., Cassidy, H. G., and Singer, S. J. (1958). Molecular structural effects produced in proteins by reaction with succinic anhydride. Biochim. Biophys. Acta, 29, 587–593.
Hamdy, M. (1974). The nutritional value of vegetable protein. Chem. Technol., 616–622.
Hurrell, F. R. and Carpenter, K. J. (1977). Nutritional significance of crosslink formation during food processing. In “Protein Crosslinking: Nutritional and Medical Consequences”, M. Friedman, Ed., Plenum Press, New York, pp. 225–238.
Klapper, M. H. and Klotz, I. M. (1972). Acylation with dicarboxylic acid anhydrides. In “Methods in Enzymology”, C.H.W. Hirs and S. N. Timascheff, Ed., Academic Press, New York, Vol. XXV, pp. 531–536.
Koenig, N. H. (1965). Wool modification with acid anhydrides in dimethylformamide. Text. Res. J., 35, 708–715.
Koenig, N. H. and Friedman, M. (1977) Comparison of wool reactions with selected mono-and bifunctional reagents. In “Protein Crosslinking: Biochemical and Molecular Aspects”, M. Friedman, Ed., Plenum Press, New York, pp. 355–382.
Krull, L.. H. and Friedman, M. (1967a). Anionic polymerization of methyl acrylate to protein functional groups. J. Polym. Sci., A-1, 5, 2535–2546.
Krull, L. H. and Friedman, M. (1967b). Reduction of protein disulfide bonds by sodium hydride in dimethyl sulfoxide. Biochem. Biophys. Res. Commun., 29, 373–377.
Provanasal, M.M.P., Cuq, J. L. A. and Cheftel, J. C. (1975). Chemical and nutritional modifications of sunflower proteins due to alkaline processing. Formation of amino acid cross-links and isomerization of lysine residues. J. Ag. Food Chem. 23, 938–943.
Riordan, J. F. and Vallee, B. L. (1972). Acetylation. In “Methods in Enzymology”, C.H.W. Hirs and S. N. Timasheff, Eds., Academic Press, New York, Vol. XXV, pp. 494–499.
Saunders, R. M., Connor, M. A., Edwards, R. H., and Kohler, G. O. (1975). Preparation of protein concentrates from wheat shorts and wheat millrun by a wet alkaline process. Cereal Chem., 52, 93–101.
Schultz, W. G., Neuman, J. J., Schade, J. E., Morgan, J. P., Katsuyama, A. M., and Maagdengerg, H. J. (1977). Commercial feasibility of recovering tomato peeling residuals. Proc. 8th Nat’l. Symp. on Food Processing Wastes.
Seattle WA, Industrial Environmental Research Laboratory, Office of Res. and Dev., U.S. Environmental Protection Agency, Cincinnati, pp 119–136.
Shapiro, R., and Gazit, A. (1977). Crosslinking of nucleic acids and proteins by bisulfite. In “Protein Crosslinking: Nutritional and Medical Consequences”, M. Friedman, Ed., Plenum Press, New York, 633–640.
Snow, J. T., Finley, J. W., and Friedman, M. (1976). Relative reactivities of sulfhydryl groups with N-acetyl dehydroalanine and N-acetyldehydroalanine methyl ester. Int. J. Peptide Protein Res., 5, 177–186.
Sternberg, M., and Kim, C. Y. (1977). Lysinoalanine formation in protein food ingredients. In “Protein Crosslinking: Nutritional and Medical Consequences”, M. Friedman, Ed., Plenum Press, New York, pp. 73–84.
Til, H. P., Feron, V. J., and DeGroot, A. P. (1972). Toxicity of sulfite. I. Long-term feeding and multigeneration studies in rats. Food Cosmet. Zbxcol., 10, (3) 291–310.
Whitaker, J. R. and Feeney, R. E. (1977). Behaviour of 0-glycosyl and 0-phosphoryl proteins in alkaline solution. In “Protein Crosslinking: Nutritional and Medical Consequences”, M. Friedman, Ed., Plenum Press, New York, pp. 155–175.
Woodard, C. J., Short, D. D., Alvarez, M. R. and Reyniers, J. (1975). Biologic effects of NE-(DL-2-amino-2-carboxyethyl)-Lr lysine, lysinoalanine. In “Protein Nutritional Quality of Foods and Feeds”, M. Friedman, Ed., Marcel Dekker, New York, pp. 595–616.
Wu, Y. V., Sexson, K. R., Cluskey, J. E. and Inglett, G. E. (1977). Protein isolates from high protein oats preparation. Composition and properties. J. Food Sci., 42, (5), 1383–1386.
Wu, Y. V., Cluskey, J. E., Krull, L. H., and Friedman, M. (1971). Some optical properties of S-ß-(4-pyridylethyl)-L-cysteine and its wheat gluten and serum albumin derivatives, Canad. J. Biochem., 49, 1042–1049.
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1978 Plenum Press, New York
About this chapter
Cite this chapter
Friedman, M. (1978). Inhibition of Lysinoalanine Synthesis by Protein Acylation. In: Friedman, M. (eds) Nutritional Improvement of Food and Feed Proteins. Advances in Experimental Medicine and Biology, vol 105. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-3366-1_30
Download citation
DOI: https://doi.org/10.1007/978-1-4684-3366-1_30
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4684-3368-5
Online ISBN: 978-1-4684-3366-1
eBook Packages: Springer Book Archive