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Aminosäuren, Peptide, Proteine

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Zusammenfassung

Aminosäuren, Peptide und Proteine sind wichtige Bestandteile von Lebensmitteln. Sie liefern einerseits die für die Proteinbiosynthese notwendigen Bausteine. Andererseits tragen Aminosäuren und Peptide direkt zum Geschmack von Lebensmitteln bei und sind auch Vorläufer für Aromastoffe und Farbstoffe, die über thermische und/oder enzymatische Reaktionen bei der Gewinnung, Verarbeitung und Lagerung von Lebensmitteln gebildet werden. An solchen Reaktionen können auch andere Lebensmittelinhaltsstoffe, z. B. Kohlenhydrate, beteiligt sein. Weiterhin tragen Proteine über ihre Fähigkeit zur Bildung oder Stabilisierung von Gelen, Schäumen, Teigen, Emulsionen und fibrillären Strukturen ganz wesentlich zu den physikalischen Eigenschaften von Lebensmitteln bei.

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Literatur

  • Aeschbach, R., Amado, R., Neukom, H.: Formation of dityrosine cross-links in proteins by oxidation of tyrosine residues. Biochim. Biophys. Acta 439, 292 (1976)

    Article  CAS  Google Scholar 

  • Arai, S., Yamashita, M., Fujimaki, M.: Nutritional improvement of food proteins by means of the plastein reaction and its novel modification. Adv. Exp. Med. Biol. 105, 663 (1978)

    Article  CAS  Google Scholar 

  • Ariyoshi, Y.: The structure-taste relationships of aspartyl dipeptide esters. Agric. Biol. Chem. 40, 983 (1976)

    Article  CAS  Google Scholar 

  • Aso, K., Yamashita, M., Arai, S., Suzuki, J., Fujimaki, M.: Specificity for incorporation of a-amino acid esters during the plastein reaction by papain. J. Agric. Food Chem. 25, 1138 (1977)

    Article  CAS  Google Scholar 

  • Belitz, H.-D., Wieser, H.: Zur Konfigurationsabhängigkeit des süßen oder bitteren Geschmacks von Aminosäuren and Peptiden. Z. Lebensm. Unters. Forsch. 160, 251 (1976)

    Article  CAS  Google Scholar 

  • Bodanszky, M.: Peptide Chemistry. Springer-Verlag: Berlin, 1988

    Book  Google Scholar 

  • Boggs, R. W.: Biovailability of acetylated derivatives of methionine, threonine and lysine. Adv. Exp. Med. Biol. 105, 571 (1978)

    Article  CAS  Google Scholar 

  • Bosin, T. R., Krogh, S., Mais, D.: Identification and quantitation of 1,2,3,4-Tetrahydro-ß-carboline-3carboxylic acid and 1-methyl-1,2,3,4-tetrahydro-43carboline-3-carboxylic acid in beer and wine. J. Agric. Food Chem. 34, 843 (1986)

    Article  CAS  Google Scholar 

  • Bott, R. R., Davies, D. R.: Pepstatin binding to Rhizopus chinensis aspartyl proteinase. In: Peptides: Structure and function (Eds.: Hruby, V. J., Rich, D. H. ), p. 531. Pierce Chemical Co.: Rockford, Ill. 1983

    Google Scholar 

  • Brussel, L. B. P., Peer, H. G., van der Heijden, A.: Structure-taste relationship of some sweet-tasting dipeptide esters. Z. Lebensm. Unters. Forsch. 159, 337 (1975)

    Article  CAS  Google Scholar 

  • Chen, C., Pearson, A.M., Gray, J. I.: Meat Mutagens. Adv. Food Nutr. Res. 34, 387 (1990)

    CAS  Google Scholar 

  • Cherry, J. P. (Ed.): Protein functionality in foods. ACS Symposium Series 147, American Chemical Society: Washington, D.C. 1981

    Google Scholar 

  • Creighton, T. E.: Proteins: structures and molecular properties. W. H. Freeman and Co.: New York. 1983

    Google Scholar 

  • Croft, L. R.: Introduction to protein sequence analysis, 2nd edn., John Wiley and Sons, Inc.: Chichester. 1980

    Google Scholar 

  • Dagleish, D.G.: Adsorptions of protein and the stability of emulsions. Trends Food Sci. Technol. 8, 1 (1997)

    Google Scholar 

  • Dickinson, E.: Towards more natural emulsifiers. Trends Food Sci. Technol. 4, 330 (1993)

    CAS  Google Scholar 

  • Einsele, A.: Biomass from higher n-alkanes. In:Biotechnology (Eds.: Rehm, H.-J., Reed, G.), Vol. 3, p. 43, Verlag Chemie: Weinheim. 1983

    Google Scholar 

  • Faust, U., Präve, P.: Biomass from methane and methanol. In: Biotechnology (Eds.: Rehm, H.-J., Reed, G.), Vol. 3, p. 83, Verlag Chemie: Weinheim. 1983

    Google Scholar 

  • Felton, J.S., Pais, P., Salmon, C.P., Knize, M.G.: Chemical analysis and significance of heterocyclic aromatic amines. Z. Lebensm. Unters. Forsch. A 207, 434 (1998)

    Article  CAS  Google Scholar 

  • Finot, P.-A., Mottu, F., Bujard, E., Mauron, J.: N-Substituted lysines as sources of lysine in nutrition. Adv. Exp. Med. Biol. 105, 549 (1978)

    Article  CAS  Google Scholar 

  • Fujino, M., Wakimasu, M., Tanaka, K., Aoki, H., Nakajima, N.: L-Aspartyl-aminomalonic acid diesters. Naturwissenschaften 60, 351 (1973)

    Article  CAS  Google Scholar 

  • Galembeck, F., Ryan, D. S., Whitaker, J. R., Feeney, R. E.: Reactions of proteins with formaldehyde in the presence and absence of sodium borohydride. J. Agric. Food Chem. 25, 238 (1977)

    Article  CAS  Google Scholar 

  • Glazer, A. N.: The chemical modification of proteins by group-specific and site-specific reagents. In: The proteins (Eds.: Neurath, H., Hill, R. L., Boeder, C.-L.), 3rd edn., Vol. II, p. 1, Academic Press: New York. 1976

    Google Scholar 

  • Grant, D. R.: The modification of wheat fluor proteins with succinic anhydride. Cereal Chem. 50, 417 (1973)

    CAS  Google Scholar 

  • Gross, E., Morell, J. L.: Structure of nisin. J. Am. Chem. Soc. 93, 4634 (1971)

    Article  CAS  Google Scholar 

  • Herderich, M., Gutsche, B.: Tryptophan-derived bio-active compounds in food. Food Rev. Int. 13, 103 (1997)

    CAS  Google Scholar 

  • Hudson, B. J. F. (Ed.): Developments in food proteins-1 ff, Applied Science Publ.: London. 1982 ff

    Google Scholar 

  • Ikenaka, T., Odani, S., Koide, T.: Chemical structure and inhibitory activities of soybean proteinase inhibitors. Bayer-Symposium V „Proteinase inhibitors“, p. 325, Springer-Verlag: Berlin. 1974

    Google Scholar 

  • Jägerstad, M., Skog, K., Arvidson, P., Solyakov, A.: Chemistry, formation and occurrence of genotoxic heterocyclic amines identified in model systems and cooked foods. Z. Lebensm. Unters. Forsch A 207, 419 (1998)

    Article  Google Scholar 

  • Kasai, H., Yamaizumi, Z., Shiomi, T., Yokoyama, S., Miyazawa, T., Wakabayashi, K., Nagao, M., Sugimura, T., Nishimura, S.: Structure of a potent mutagen isolated from fried beef. Chem. Lett. 1981, 485

    Google Scholar 

  • Kasai, H., Yamaizumi, Z., Wakabayashi, K., Nagao, M., Sugimura, T., Yokoyama, S., Miyazawa, T., Spingarn, N. E., Weisburger, J.H., Nishimura, S.: Potent novel mutagens produced by broiling fish under normal conditions. Proc. Jpn. Acad. Ser. B 56, 278 (1980)

    Article  CAS  Google Scholar 

  • Kessler, H. G.: Lebensmittel-and Bioverfahrenstechnik; Molkereitechnologie. 3. Auflage. Verlag A. Kessler: Freising, 1988

    Google Scholar 

  • Kinsella, J. E., Shetty, K. J.: Yeast proteins: Recovery and functional properties. Adv. Exp. Med. Biol. 105, 797 (1978)

    Article  CAS  Google Scholar 

  • Kinsella, J. E.: Functional properties of proteins in foods: A survey. Crit. Rev. Food Sci. Nutr. 7, 219 (1976)

    Article  CAS  Google Scholar 

  • Kinsella, J. E.: Texturized proteins: Fabrication, flavoring, and nutrition. Crit. Rev. Food Sci. Nutr. 10, 147 (1978)

    Article  CAS  Google Scholar 

  • Kleemann, A., Leuchtenberger, W, Hoppe, B., Tanner, H.: Amino acids. In: Ullmann’s encyclopedia of industrial chemistry, 5th Edition, Volume A2, p. 57, Verlag VCA, Weinheim, 1986

    Google Scholar 

  • Klostermeier, H., et al.: Proteins. In: Ullmann’s encyclopedia of industrial chemistry, 5th Edition, Volume A22, p. 289, Verlag VCH, Weinheim, 1993

    Google Scholar 

  • Kostka, V. (Ed.): Aspartic proteinases and their inhibitors. Walter de Gruyter: Berlin. 1985

    Google Scholar 

  • Läsztity, R.: Rheologische Eigenschaften von Weizenkleber und ihre Beziehungen zu molekularen Parametern. Nahrung 19, 749 (1975)

    Article  Google Scholar 

  • Li-Chan, E., Helbig, N., Holbek, E., Chau, S., Nakai, S.: Covalent attachment of lysine to wheat gluten for nutritional improvement. J. Agric. Food Chem. 27, 877 (1979)

    Article  CAS  Google Scholar 

  • Lottspeich, F., Henschen, A., Hupe, K.-P. (Eds.): High performance liquid chromatography in protein and peptide chemistry. Walter de Gruyter: Berlin. 1981

    Google Scholar 

  • Lübke, K., Schröder, E., Kloss, G.: Chemie und Biochemie der Aminosäuren, Peptide und Proteine. Georg Thieme Verlag: Stuttgart. 1975

    Google Scholar 

  • Masters, P. M., Friedman, M.: Racemization of amino acids in alkali-treated food proteins. J. Agric. Food Chem. 27, 507 (1979)

    Article  CAS  Google Scholar 

  • Mauron, J.: Ernährungsphysiologische Beurteilung bearbeiteter Eiweißstoffe. Dtsch. Lebensm. Rundsch. 71, 27 (1975)

    CAS  Google Scholar 

  • Mazur, R. H., Goldkamp, A. H., James, P. A., Schlatter, J. M.: Structure-taste relationships of aspartic acid amides. J. Med. Chem. 13, 1217 (1970)

    Article  CAS  Google Scholar 

  • Mazur, R. H., Reuter, J. A., Swiatek, K. A., Schlatter, J. M.: Synthetic sweeteners 3. Aspartyl dipeptide esters from L- and D-alkylglycines. J. Med. Chem. 16, 1284 (1973)

    Article  CAS  Google Scholar 

  • Meister, A.: Biochemistry of the amino acid. 2nd edn., Vol. I, Academic Press: New York. 1965

    Google Scholar 

  • Morrissay, P. A., Mulvihill, D.M., O’Neill, E.M.: Functional properties of muscle proteins. In: Development in Food Proteins — 5; (Ed.: Hudson, B.J. F. ), p. 195, Elsevier Applied Science: London. 1987

    Google Scholar 

  • Nagao, M., Yahagi, T., Kawachi, T., Seino, Y., Honda, M., Matsukura, N., Sugimura, T., Wakabayshi, K., Tsuji, K., Kosuge, T.: Mutagens in foods, and especially pyrolysis products of protein. Dev. Toxicol. Environ. Sci. 2nd (Frog. Genet. Toxicol.), p. 259 (1977)

    Google Scholar 

  • Nakai, S., Modler, H.W.: Food proteins. Properties and characterization. Verlag Chemie, Weinheim, 1996.

    Google Scholar 

  • Oura, E.: Biomass from carbohydrates. In: Biotechnology (Eds.: Rehm, H.-J., Reed, G.), Vol. 3, p. 3, Verlag Chemie: Weinheim. 1983

    Google Scholar 

  • Pence, J.W., Mohammad, A., Mecham, D.K.: Heat denaturation of gluten. Cereal Chem. 30, 115 (1953)

    CAS  Google Scholar 

  • Perutz, M. F.: Proteins and nucleic acids. Elsevier Publ. Co.: Amsterdam. 1962

    Google Scholar 

  • Phillips, E.G., Whitehead, D.M., Kinsella, J.: Structure-function properties of food proteins. Academic Press, London, 1994.

    Google Scholar 

  • Poindexter, E. H., Jr., Carpenter, R. D.: Isolation of harmane and norharmane from cigarette smoke. Chem. Ind. 1962, 176

    Google Scholar 

  • Puigserver, A. J., Sen, L. C., Clifford, A. J., Feeney, R. E., Whitaker, J. R.: A method for improving the nutritional value of food proteins: Covalent attachment of amino acids. Adv. Exp. Med. Biol. 105, 587 (1978)

    Article  CAS  Google Scholar 

  • Repley, J. A., Careri, G.: Protein hydration and function. Adv. Protein Chem. 41, 38 (1991)

    Google Scholar 

  • Richmond, A.: Phototrophic microalgae. In: Biotechnology (Eds.: Rehm, H.-J., Reed, G.), Vol. 3, p. 109, Verlag Chemie: Weinheim. 1983

    Google Scholar 

  • Schulz, G. E., Schirmer, R. H.: Principle of protein structure. Springer-Verlag: Berlin. 1979

    Book  Google Scholar 

  • Schmitz, M.: Möglichkeiten und Grenzen der Homoarginin-Markierungsmethode zur Messung der Proteinverdaulichkeit beim Schwein. Dissertation, Universität Kiel. 1988

    Google Scholar 

  • Schwenke, K. D.: Beeinflussung funktioneller Eigenschaften von Proteinen durch chemische Modifizierung. Nahrung 22, 101 (1978)

    Article  CAS  Google Scholar 

  • Seki, T., Kawasaki, Y., Tamura, M., Tada, M., Okai, H.: Further study on the salty peptide ornithy1- I-alanine. Some effects of pH and additive ions on saltiness. J. Agric. Food Chem. 38, 25 (1990)

    Article  CAS  Google Scholar 

  • Severin, Th., Ledl, F.: Thermische Zersetzung von Cy-stein in Tributyrin. Chem. Mikrobiol. Technol. Lebensm. 1, 135 (1972)

    CAS  Google Scholar 

  • Shinoda, I., Tada, M., Okai, H.: A new salty peptide, ornithyl-13-alanine hydrochloride. Pept. Chem., 21st. Proceeding of the Symposium on Peptide Chemistry 1983, p. 43 (1984)

    Google Scholar 

  • Soda, K., Tanaka, H., Esaki, N.: Amino acids. In: Biotechnology (Eds.: Rehm, H.-J., Reed, G.), Vol. 3, p. 479, Verlag Chemie: Weinheim. 1983

    Google Scholar 

  • Sternberg, M., Kim, C.Y.: Lysinoalanine formation in protein food ingredients. Adv. Exp. Med. Biol. 86B, 73 (1977)

    Google Scholar 

  • Sugimura, T., Kawachi, T., Nagao, M., Yahagi, T., Seino, Y., Okamoto, T., Shudo, K., Kosuge, T.,Tsuji, K. et al.: Mutagenic principle(s) in tryptophan and phenylalanine pyrolysis products. Proc. Jpn. Acad. 53, 58 (1977)

    CAS  Google Scholar 

  • Sulser, H.: Die Extraktstoffe des Fleisches. Wissenschaftliche Verlagsgesellschaft mbH: Stuttgart. 1978

    Google Scholar 

  • Traub, W., Piez, K. A.: The chemistry and structure of collagen. Adv. Protein Chem. 25, 267 (1971)

    Google Scholar 

  • Treleano, R., Belitz, H.-D., Jugel, H., Wieser, H.: Beziehungen zwischen Struktur und Geschmack bei Aminosäuren mit cyclischen Seitenketten. Z. Lebensm. Unters. Forsch. 167, 320 (1978)

    Article  CAS  Google Scholar 

  • Tschesche, H. (Ed.): Modern Methods in Protein Chemistry, Vol. 2, Walter de Gruyter: Berlin. 1985

    Google Scholar 

  • Voutsinas, L. P., Nakai, S.: Covalent binding of methionine and tryptophan to soy protein. J. Food Sci. 44, 1205 (1979)

    Article  CAS  Google Scholar 

  • Walton, A. G.: Polypeptides and protein structure, Elsevier North Holland, Inc., New York. 1981

    Google Scholar 

  • Watanabe, M., Arai, S.: The plastein reaction and its applications. In: Developments in Food Proteins — 6; (Ed.: Hudson, B. J. F. ), p. 179, Elsevier Applied Science: London. 1988

    Google Scholar 

  • Whitaker, J. F., Fujimaki, M. (Eds.): Chemical deterioration of proteins, ACS Symposium Series 123, American Chemical Society: Washington, D.C. 1980

    Google Scholar 

  • Wieser, H., Belitz, H.-D.: Zusammenhänge zwischen Struktur und Bittergeschmack bei Aminosäuren und Peptiden. I. Aminosäuren und verwandte Verbindungen. Z. Lebensm. Unters. Forsch. 159, 65 (1975)

    Article  CAS  Google Scholar 

  • Wieser, H., Belitz, H.-D.: Zusammenhänge zwischen Struktur und Bittergeschmack bei Aminosäuren und Peptiden. II. Peptide und Peptidderivate. Z. Lebensm. Unters. Forsch. 160, 383 (1976)

    Article  CAS  Google Scholar 

  • Wieser, H., Jugel, H., Belitz, H.-D.: Zusammenhänge zwischen Struktur und Süßgeschmack bei Aminosäuren. Z. Lebensm. Unters. Forsch. 164, 277 (1977)

    Article  CAS  Google Scholar 

  • Wild, D., Kerdar, R.S.: The inherent genotoxic potency of food mutagens and other heterocyclic and carboxylic aromatic amines and corresponding azides. Z. Lebensm. Unters. Forsch. A 207, 428 (1998)

    Article  CAS  Google Scholar 

  • Wittmann-Liebold, B., Salnikow, J., Erdmann, V.A. (Eds.): Advanced Methods in Protein Microsequence Analysis. Springer-Verlag: Berlin. 1986

    Google Scholar 

  • Yamashita, M., Arai, S., Fujimaki, M.: A low-phenylalanine, high-tyrosine plastein as an acceptable dietetic food. J. Food Sci. 41, 1029 (1976)

    Article  CAS  Google Scholar 

  • Yamashita, M., Arai, S., Amano, Y., Fujimaki, M.: A novel one-step process for enzymatic incorporation of amino acids into proteins: Application to soy protein and flour for enhancing their methionine levels. Agric. Biol. Chem. 43, 1065 (1979)

    Article  CAS  Google Scholar 

  • Yamashita, M., Arai, S., Tsai, S.-J., Fujimaki, M.: Plastein reaction as a method for enhancing the sulfur-containing amino acid level of soybean protein. J. Agric. Food Chem. 19, 1151 (1971)

    Article  CAS  Google Scholar 

  • Yamashita, M., Arai, S., Kokubo, S., Aso, K., Fuji-maki, M.: Synthesis and characterization of a glutamic acid enriched plastein with greater solubility. J. Agric. Food Chem. 23, 27 (1975)

    Article  CAS  Google Scholar 

  • Yoshikawa, M., Tamaki, M., Sugimoto, E., Chiba, H.: Effect of dephosphorylation on the self-association and the precipitation of I-Casein. Agric. Biol. Chem. 38, 2051 (1974)

    Article  CAS  Google Scholar 

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  1. Technischen Universität München, Lichtenbergstraße 4, 85748, Garching, Deutschland

    Professor Dr. Werner Grosch (Außerplanmäßiger Professor für Lebensmittelchemie, Ehem. stellvertr. Direktor der Deutschen Forschungsanstalt für Lebensmittelchemie München) & Professor Dr. Peter Schieberle (Ordinarius für Lebensmittelchemie, Leiter des Instituts für Lebensmittelchemie, Direktor der Deutschen Forschungsanstalt für Lebensmittelchemie München)

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  1. Professor Dr. Hans-Dieter Belitz
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  2. Professor Dr. Werner Grosch
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  3. Professor Dr. Peter Schieberle
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Belitz, HD., Grosch, W., Schieberle, P. (2001). Aminosäuren, Peptide, Proteine. In: Lehrbuch der Lebensmittelchemie. Springer-Lehrbuch. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-662-08302-4_2

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  • DOI: https://doi.org/10.1007/978-3-662-08302-4_2

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