- 1) Bloksma, A. H., and Bushuk, W., Rheology and chemistry of dough. In “Wheat: Chemistry and Technology” third ed. Vol. II, ed. Pomeranz, Y., American Association of Cereal Chemists, Minnesota, pp. 131–217 (1988).
- 2) Takasaki, S., and Kawakishi, S., Formation of protein-bound 3,4-dihydroxyphenylalanine and 5-S-cysteinyl-3,4-dihydroxyphenylalanine as new cross-linkers in gluten. J. Agric. Food Chem., 45, 3472–3475 (1997).
- 3) Takasaki, S., and Kawakishi, S., Effects of polyphenol oxidase activity in wheat flour on protein-bound 5-S-cysteinyldopa formation in gluten. Food Sci. Technol. Res., 6, 40–43 (2000).
- 4) Takasaki, S., Kawakishi, S., Murata, M., and Homma, S., Polymerisation of gliadin mediated by mushroom tyrosinase. Lebensm.-Wiss. u.-Technol., 34, 507–512 (2001).
- 5) Tilley, K. A., Benjamin, R. E., Bagorogoza, K. E., Okot-Kotber, B. M., Prakash, O., and Kwen, H., Tyrosine cross-links: molecular basis of gluten structure and function. J. Agric. Food Chem., 49, 2627–2632 (2001).
- 6) Amadò, R., Aeschbach, R., and Neukom, H., Dityrosine: in vitro production and characterization. Methods Enzymol., 107, 377–388 (1984).
- 7) Aeschbach, R., Amadò, R., and Neukom, H., Formation of dityrosine cross-links in protein by oxidation of tyrosine residues. Biochim. Biophys. Acta, 439, 292–301 (1976).
- 8) Malencik, D. A., and Anderson, S. R., Dityrosine formation in calmodulin: cross-linking and polymerization catalyzed by Arthromyces peroxidase. Biochemistry, 35, 4375–4386 (1996).
- 9) Kikugawa, K., Kato, T., and Hayasaka, A., Formation of dityrosine and other fluorescent amino acids by reaction of amino acids with lipid hydroperoxides. Lipids, 26, 922–929 (1991).
- 10) Heinecke, J. W., Li, W., Daehnke, H. L., III, and Goldstein, J. A., Dityrosine, a specific marker of oxidation, is synthesized by the myeloperoxidase-hydrogen peroxide system of human neutrophils and macrophages. J. Biol. Chem., 268, 4069–4077 (1993).
- 11) Kato, Y., Uchida, K., and Kawakishi, S., Aggregation of collagen exposed to uva in the presence of riboflavin: a plausible role of tyrosine modification. Photochem. Photobiol., 59, 343–349 (1994).
- 12) Michon, T., Wang, W., Ferrasson, E., and Guéguen, J., Wheat prolamine crosslinking through dityrosine formation catalyzed by peroxidases: improvement in the modification of a poorly accessible substrate by “indirect” catalysis. Biotechnol. Bioeng., 63, 449–458 (1999).
- 13) Michon, T., Chenu, M., Kellershon, N., Desmadril, M., and Guéguen, J., Horseradish peroxidase oxidation of tyrosine-containing peptides and their subsequent polymerization: a kinetic study. Biochemistry, 36, 8504–8513 (1997).
- 14) Kieffer, R., Matheis, G., Hofmann, H. W., and Belitz, H.-D., Verbesserung der backeigenschaften von weizenmehlen durch zusätze von peroxidase aus meerrettich, H2O2 und phenolen. Z. Lebensm. Unters. Forsch., 173, 376–379 (1981).
- 15) Liao, Y., Miller, R. A., and Hoseney, R. C., Role of hydrogen peroxide produced by baker’s yeast on dough rheology. Cereal Chem., 75, 612–616 (1998).
- 16) Delcros, J.-F., Rakotozafy, L., Boussard, A., Davidou, S., Porte, C., Potus, J., and Nicolas, J., Effect of mixing conditions on the behavior of lipoxygenase, peroxidase, and catalase in wheat flour doughs. Cereal Chem., 75, 85–93 (1998).
- 17) Bhattacharjee, S., Pennathur, S., Byun, J., Crowley, J., Mueller, D., Gischler, J., Hotchkiss, R. S., and Heinecke, J. W., NADPH oxidase of neutrophils elevates o.o′-dityrosine cross-links in proteins and urine during inflammation. Arch. Biochem. Biophys., 395, 69–77 (2001).
- 18) Fenaille, F., Parisod, V., Vuichoud, J., Tabet, J.-C., and Guy, P. A., Quantitative determination of dityrosine in milk powders by liquid chromatography coupled to tandem mass spectrometry using isotope dilution. J. Chromatogr. A, 1052, 77–84 (2004).
- 19) Pomeranz, Y., Chemical composition of kernel structures. In “Wheat: Chemistry and Technology” third ed. Vol. I, ed. Pomeranz, Y., American Association of Cereal Chemists, Minnesota, pp. 97–158 (1988).
- 20) Tsen, C. C., and Hlynka, I., The role of lipids in oxidation of doughs. Cereal Chem., 39, 209–219 (1962).
- 21) Neukom, H., and Markwalder, H. U., Oxidative gelation of wheat flour pentosans: a new way of cross-linking polymers. Cereal Foods World, 23, 374–376 (1978).
- 22) Matheis, G., and Whitaker, J. R., Peroxidase-catalyzed cross linking of proteins. J. Protein Chem., 3, 35–48 (1984).
- 23) Figueroa-Espinoza, M.-C., Morel, M.-H., Surget, A., and Rouau, X., Oxidative cross-linking of wheat arabinoxylans by manganese peroxidase. Comparison with laccase and horseradish peroxidase. Effect of cysteine and tyrosine on gelation. J. Sci. Food Agric., 79, 460–463 (1999).
- 24) Hoseney, R. C., and Faubion, J. M., A mechanism for the oxidation gelation of wheat flour water-soluble pentosans. Cereal Chem., 58, 421–424 (1981).
Bioscience, Biotechnology, and Biochemistry
Volume 69, 2005 - Issue 9