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• W2122768125 abstract "Journal of Food BiochemistryVolume 23, Issue 4 p. 367-407 RECENT PROGRESS IN PROCESSING OF DAIRY PROTEINS: A REVIEW THOMAS HAERTLÉ, THOMAS HAERTLÉ Institut National de la Recherche Agronomique Laboratoire d'Etude des Interactions des Molécules Alimentaires B.P. 71627, 44316 Nantes Cedex 3, FranceSearch for more papers by this authorJEAN-MARC CHOBERT, Corresponding Author JEAN-MARC CHOBERT Institut National de la Recherche Agronomique Laboratoire d'Etude des Interactions des Molécules Alimentaires B.P. 71627, 44316 Nantes Cedex 3, France1 corresponding author: fax: 332.40.67.50.84, e-mail: [email protected]Search for more papers by this author THOMAS HAERTLÉ, THOMAS HAERTLÉ Institut National de la Recherche Agronomique Laboratoire d'Etude des Interactions des Molécules Alimentaires B.P. 71627, 44316 Nantes Cedex 3, FranceSearch for more papers by this authorJEAN-MARC CHOBERT, Corresponding Author JEAN-MARC CHOBERT Institut National de la Recherche Agronomique Laboratoire d'Etude des Interactions des Molécules Alimentaires B.P. 71627, 44316 Nantes Cedex 3, France1 corresponding author: fax: 332.40.67.50.84, e-mail: [email protected]Search for more papers by this author First published: 23 February 2007 https://doi.org/10.1111/j.1745-4514.1999.tb00027.xCitations: 19AboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL References AESCHLIMANN, D. and PAULSSON, M. 1994. Transglutaminase: Protein cross-linking enzyme in tissues and body fluids. Thromb. Haemost. 71, 402– 415. ANTILA, P., PAAKARI, I., JÄRVINEN, A., MATTILA, M.J., LAUKKANEN, M., PIHHLANTO-LEPPÄLÄ, A., MÄNTSÄLÄ, P. and HELLMAN J. 1991. Opioid peptides derived from in vitro proteolysis of bovine whey proteins. Int. Dairy J. 1, 215– 229. ARAKI, H. and SEKI, N. 1993. Comparison of reactivity of transglutaminase to various fish actomyosin. Bull. Jap. Soc. Sci. Fish. 59, 711– 716. AZUAGA, A.I., GALISTEO, M.L., MAYORGA, O.L., CORTIJO, M. and MATEO, P.L. 1992. Heat and cold denaturation of ß-lactoglobulin B. FEBS Lett. 309, 258– 260. BALNY, C. and MASSON, P. 1993. Effects of pressure on proteins. Food Rev. Intern. 9, 611– 628. BARBU, E., BASSET, J. and JOLY, M. 1954. Action des hautes pressions sur la sérum-albumine de chevalEtude. par la biréfrigence d'écoulement. Bull. Soc. Chim. Biol. 36, 323– 333. BARBU, E. and MACHEBOEUF, M. 1948. Recherches sur la gélification des protéines. 5. Considérations générales et interprétations. Ann. Inst. Pasteur 75, 426– 441. BATT, C.A. 1997. Genetic engineering of food proteins. In Food Proteins and their Applications. ( S. Damodaran and A. Paraf, eds.) pp. 425– 441, Marcel Dekker, New York . BAUM, J., DOBSON, C.M, EVANS, P.A. and HANLEY, C. 1989. Characterization of a partly folded protein by NMR methods: Studies on the molten globule state of guinea pig α-lactalbumin. Biochemistry 28, 7– 13. BERTRAND-HARB, C., CHARRIER, B., DALGALARRONDO, M., CHOBERT, J.M. and HAERTLÉ, T. 1990. Condensation of glycosidic and aromatic structures on amino groups of beta-lactoglobulin via reductive alkylation. Lait 71, 205– 215. BORCH, R.F., BERNSTEIN, M.D. and DURST D.H. 1971. The cyanohydroborate anion as selective reducing agent. J. Am. Chem. Soc. 93, 2897– 2904. BOUHALLAB, S., SAPIN, B., MOLLÉ, D. HENRY, G. and LÉONIL, J. 1997. Inhibition of bovine trypsin by the phosphorylated N-terminal part ß (1–105) of ß-casein. J. Peptide Res. 49, 23– 27. BOYER, P.D. 1954. Reaction of protein sulfhydryl groups with organic mercurials. J. Amer. Chem. Soc. 76, 4331– 4337. BRANTL, V., TESCHEMACHER, H, HENSCHEN, A. and LOTTSPEICH, F. 1979. Opioid activities of ß-casomorphins. Hoppe-Seyler's Z. Physiol. Chem. 360, 1211– 1216. BRIAND, L., CHOBERT, J.M., GANTIER, R., DECLERCK, N., TRAN, V., LÉONIL, J., MOLLÉ, D. and HAERTLÉ, T. 1999. Impact of the Lysine-188 and Aspartic Acid-189 inversion on activity of trypsin. FEBS Lett. 442, 43– 47. BRIAND, L., CHOBERT, J.M. and HAERTLÉ, T. 1995. Peptic proteolysis of esterified ß-casein and ß-lactoglobulin. Int. J. Peptide Protein Res. 46, 30– 36. BRIAND, L., CHOBERT, J.M., TAUZIN, J., DECLERCK, N., LÉONIL, J., MOLLÉ, D., TRAN, V. and HAERTLÉ, T. 1997. Regulation of trypsin activity by a Cu2+ chelation of the substrate binding site. Prot. Eng. 10, 551– 560. BRIDGMAN, P.W. 1914. The coagulation of albumins by pressure. J. Biol. Chem. 19, 511– 512. BUROVA, T.V., CHOISET, Y, TRAN, V. and HAERTLÉ, T. 1998a. Role of free Cys121 in stabilization of bovine ß-lactoglobulin B. Prot. Eng. 11, 1065– 1073. BUROVA, T.V., GRINBERG, V. Ya., TRAN, V. and HAERTLÉ, T. 1998b. What may be bovine ß-lactoglobulin Cys 121 good for Int. Dairy J. 8, 83– 86. CABACUNGAN, J.C., AHMED, A.I. and FEENEY, R.E. 1982. Amine boranes as alternative reducing agents for reductive alkylation. Anal. Biochem. 124, 272– 278. CHO, Y., GU, W., WATKINS, S., LEE, S.P., BRADY, J.W. and BATT, C.A. 1994. Thermostable variants of bovine ß-lactoglobulin. Prot. Eng. 7: 263. CHOBERT, J.M., BERTRAND-HARB, C., NICOLAS, M.G., GAERTNER, H. and PUIGSERVER, A., 1987. Solubility and emulsifying property of caseins chemically modified by covalent attachment of L-methionine and L-valine. J. Agric. Food Chem. 35, 638– 644. CHOBERT, J.M., BERTRAND-HARB, C, DALGALARRONDO, M. and NICOLAS, M.G. 1989a. Solubility and emulsifying properties of ß-casein modified enzymatically by trypsin. J. Food Biochemistry 13, 335– 352. CHOBERT, J.M., BRIAND, L., GRINBERG, V. Ya and HAERTLÉ, T. 1995. Impact of esterification on the folding and the susceptibility to peptic proteolysis of ß-lactoglobulin. Biochim. Biophys. Acta 1248, 170– 176. CHOBERT, J.M., BRIAND, L. and HAERTLÉ, T. 1993. Procédé d'obtention de populations peptidiques et produits obtenus. French Patent No. 93 15764. CHOBERT, J.M., BRIAND, L. and HAERTLÉ, T. 1998a. Influence of G187W/K188F/D189Y mutation in the substrate binding pocket of trypsin on ß-casein processing. J. Food Biochemistry 22, 529– 545. CHOBERT, J.M., BRIAND, L., LÉONIL, J., MOLLÉ, D. and HAERTLÉ, T. 1998b. Engineering of trypsin and its impact on ß-casein processing. Nahrung 42, 135– 138. CHOBERT, J.M., BRIAND, L, TRAN, V. and HAERTLÉ, T. 1998c. How the substitution of K188 of trypsin binding site by aromatic amino acids can influence the processing of ß-casein. Biochim. Biophys. Res. Commun. 246, 847– 858. CHOBERT, J.M., SITOHY, M. and WHITAKER, J.R. 1989b. Covalent attachment of phosphate and amino acids to zein. Sci. Aliments 9, 749– 761. CHOBERT, J.M., TOUATI, A., BERTRAND-HARB, C., DALGALARRONDO, M., NICOLAS, M.G. and HAERTLÉ, T. 1990. Ethyl-substituted ß-caseinStudy. of differences between esterified and reductively alkylated ß-casein derivatives. J. Agric. Food Chem. 38, 1321– 1326. COURTHAUDON, J.L., COLAS, B. and LORIENT, D. 1989. Covalent binding of glycosyl residues to bovine casein: effects on solubility and viscosity. J. Agric. Food Chem. 37, 32– 36. CUNNINGHAM, L.W. and NUENKE, B.J. 1959. Physical and chemical studies of a limited reaction of iodine with proteins. J. Biol. Chem. 234, 1447– 1451. CUNNINGHAM, L.W. and NUENKE, B.J. 1960. Analysis of modified ß-lactoglobulins and ovalbumins prepared from sulfenyl iodide intermediates. J. Biol. Chem. 235, 1711– 1715. DALGALARRONDO, M., CHOBERT, J.M., DUFOUR, E., BERTRAND-HARB, C., DUMONT, J.P. and HAERTLÉ, T. 1990. Characterization of bovine ß-lactoglobulin B tryptic peptides by reversed-phase high performance liquid chromatography. Milchwissenschaft 45, 212– 216. DALGALARRONDO, M., DUFOUR, E., CHOBERT, J.M., BERTRAND-HARB, C. and HAERTLÉ, T. 1995. Proteolysis of ß-lactoglobulin and ß-casein by pepsin in ethanolic media. Int. Dairy J. 5, 1– 14. DEFAYE, A.B. and LEDWARD, D.A. 1995. Pressure induced dimerization of metmyoglobin. J. Food Sci. 60, 262– 264. DICKINSON, E. 1992. Structure and composition of adsorbed protein layers and the relationship to emulsion stability. J. Chem. Soc., Faraday Trans. 88, 2973– 2983. DICKINSON, E. and EUSTON, S.R. 1992. Computer simulation model of the adsorption of protein-polysaccharide complexes. Food Hydrocoll. 6, 345– 357. DICKINSON, E. and GALASKA, V.B. 1991. Emulsion stabilization by ionic and covalent complexes of ß-lactoglobulin with polysaccharides. Food Hydrocoll. 5, 281– 296. DOI, E., SHIMIZU, A, OE, H. and KITABAKE, N. 1991. Melting of heat-induced ovalbumin gels by pressure. Food Hydrocoll. 5, 409– 425. DUFOUR, E., HERVE, G. and HAERTLÉ, T. 1995. Hydrolysis of ß-lactoglobulin by pepsin and thermolysin under high hydrostatic pressure. Biopolymers 35, 475– 483. DUMAY, E.M., KALICHEVSKY, M.T. and CHEFTEL, J.C. 1994. High-pressure unfolding and aggregation of ß-lactoglobulin and the baroprotective effect of sucrose. J. Agric. Food Chem. 42, 1861– 1868. EVERSHED, R.P., BLAND, H.A., van BERGEN, P.F., CARTER, J.F., HORTON, M.C. and ROWLEY-CONWY, P.A. 1997. Volatile compounds in archaeological plant remains and the Maillard reaction during decay of organic matter. Science 278, 432– 433. FEENEY, R.E. 1987. Chemical modifications of proteins: comments and perspectives. Int. J. Peptide Protein Res. 29, 145– 161. FRIEDMAN, M. 1994. Mechanisms of beneficial effects of sulfur amino acids. In Sulfur Compounds in Foods. ( C.J. Mussian and M.E. Keelan, eds.) pp. 258– 277, American Chemical Society: Washington DC . FRIEDMAN, M. 1996. Food browning and its prevention: an overview. J. Agric. Food Chem. 44, 631– 653. FUNTENBERGER, S., DUMAY, E. and CHEFTEL, J.C. 1995. Pressure-induced aggregation of β-lactoglobulin in pH 7.0 buffers. Lebensm.-Wiss. u.-Technol. 28, 410– 418. GEOGHEGAN, K.F., CABACUNGAN, J.C, DIXON, H.B.F. and FEENEY, R.E. 1981. Alternative reducing agents for reductive methylation of amino groups in proteins. Int. J. Peptide Prot. Res. 17, 345– 352. GRIKO, Yu.V. and KUTYSHENKO, V.P 1994. ß-lactoglobulin cold and heat denaturations. Biophys. J. 67, 356– 363. GROSS, M. and JAENICKE, R. 1994. Proteins under pressure. The influence of high hydrostatic pressure on structure, function and assembly of proteins and protein complexes. Eur. J. Biochem. 221, 617– 630. GUILLOU, H., MIRANDA, G. and PÉLISSIER, J.P. 1991. Hydrolysis of ß-casein by gastric proteases. 1- Comparison of proteolytic action of bovine chymosin and pepsin A. Int. J. Peptide Protein Res. 37, 494– 501. HAERTLÉ, T. and GRINBERG, V. Ya. 1996. Procédé d'homo ou d'hétéro polymérisation de protéines dotées de groupements thiols libres ou appariés en ponts disulfures. French Patent n°96 04385. HAMBLING, S.G., Mc ALPINE, A.S. and SAWYER, L. 1992. ß-Lactoglobu-lin In Advanced Dairy Chemistry -1: Protein, ( P.F. Fox, ed.) pp. 141– 190 Elsevier Applied Science, New York . HAYAKAWA, I., KAJIHARA, J., MORIKAWA, K., ODA, M. and FUJIO, Y. 1992. Denaturation of bovine serum albumin (BSA) and ovalbumin by high pressure, heat and chemicals. J. Food Sci. 57, 288– 292. HAYAKAWA, S. and NAKAMURA, R. 1986. Optimization approaches to thermally induced egg white lysozyme gel. Agric. Biol. Chem. 50, 2039– 2046. HIROTSUKA, M., TANIGUCHI, H, NARITA, H. and KITO, M. 1984. Functionality and digestibility of a highly phosphorylated soybean protein. Agric. Biol. Chem. 48, 93– 100. HOLDEN, H.M., RYPNIEWSKI, W.R, LAW, J.H. and RAYMENT, I. 1987. The molecular structure of insecticyanin from the tobacco horworm Manduca sexta L. at 2.6 Å resolution. EMBO J. 6, 1565– 1570. HUANG, Y.T. and KINSELLA, J.E. 1986. Functional properties of phosphorylated yeast proteins: solubility, water holding capacity and viscosity. J. Agric. Food Chem. 34, 670– 674. HUANG, Y.T. and KINSELLA, J.E. 1987 Effect of phosphorylation on emulsifying and foaming properties and digestibility of yeast protein. J. Food Sci. 52, 1684– 1688. HUBER, R., SCHNEIDER, M., EPP, O., MAYR, I., MESSERSCHMIDT, A.J, PLUGRATH, A. and KAYSER, H. 1987. Crystallization, crystal structure analysis and preliminary molecular model of the bilin binding protein from the insect Pieris brassicae. J. Mol. Biol. 195, 423– 434. ICEKSON, I. and APELBAUM, A. 1987. Evidence for transglutaminase activity in plant tissue. Plant Physiology 84, 972– 974. IKEGUCHI, M., KUWAJIMA, K, MITANI, M. and SUGAI, S. 1986. Evidence for identity between the equilibrium unfolding intermediate and a transient folding intermediate: A comparative study of the folding reactions of α-iactalbumin and lysozyme. Biochemistry 25, 6965– 6972. IKEGUCHI, Y., TANJI, H, KIM, K. and SUZUKI, A. 1992. Dynamic rheological measurements on heat-induced pressurized actomyosin gels. J. Agric. Food Chem. 40, 1751– 1755. JEGOUIC, M., GRINBERG, V. Ya, GUINGANT, A. and HAERTLÉ, T. 1996. Thiol-induced oligomerization of α-lactalbumin at high pressure. J. Prot. Chem. 15, 501– 509. JEGOUIC, M., GRINBERG, V. Ya, GUINGANT, A. and HAERTLÉ, T. 1997a. Baric oligomerization of α-lactalbumin/ß-lactoglobulin mixtures. J. Agric. Food Chem. 45, 19– 22. JEGOUIC, M., GRINBERG, V. Ya, GUINGANT, A. and HAERTLÉ, T. 1997b. Reducer driven baric oligomerization of α-lactalbumin. In High Pressure Research in the Biosciences and Biotechnology, ( K. Heremans, ed.) pp. 427– 430, Leuven University Press, Leuven , Belgium . JENSEN, E.V. 1959. Sulfhydryl-Disulfide Interchange. Science 130, 1319– 1323. KATO, A., MIFURU, R, MATSUDOMI, N. and KOBAYASHI, K. 1992. Functional casein-polysaccharide conjugates prepared by controlled heating. Biosci. Biotech. Biochem. 56, 567– 571. KATO, A. and NAKAI, S. 1980. Hydrophobicity determined by a fluorescence probe method and its correlation with the surface properties of proteins. Biochim. Biophys. Acta 624, 13– 20. KINSELLA, J.E. 1976. Functional properties in food: a survey. CRC Crit. Rev. Food. Sci. Nutr. 219– 280. KITABATAKE, N., CUQ, J.L. and CHEFTEL, J.C. 1985. Covalent binding of glycosylated residues of ß-lactoglobulin: effects on solubility and heat stability. J. Agric. Food Chem. 33, 125– 130. KLEIN, J.D., GUZMAN, E. and KUEHN, G.D. 1992. Purification and partial characterization of transglutaminase from Physarum polycephalum. Bacteriology 174, 2599– 2605. KRONMAN, M.J. 1989. Metal-ion binding and the molecular conformational properties of α-lactalbumin. Crit. Rev. Biochem. Mol. Biol. 24, 565– 667. LEE, H.S., SEN, L.C. and FEENEY, R.E. 1979. Preparation and nutritional properties of caseins covalently modified with sugars. Reductive alkylation of lysines with glucose, fructose and lactose. J. Agric. Food Chem. 27, 1094– 1104. LÉONIL, J., MOLLÉ, D., FAUQUANT, J., MAUBOIS, J.L, PEARCE, R.J. and BOUHALLAB, S. 1997. Characterization by ionization mass spectrometry of lactosyl ß-lactoglobulin conjugates formed during heat treatment of milk and whey and identification of one lactose-binding site. J. Dairy Sci. 80, 2270– 2281. LÉONIL, J., MOLLÉ, D. and MAUBOIS, J.L. 1988. Study of the early stages of tryptic hydrolysis of ß-casein. Lait 68, 291– 294. MAILLARD, L.C. 1912. Action des acides aminés sur les sucres; formation des mélanoïdines par voie méthodique. Compte-rendus hebdomadaires de l'Académie des Sciences 154, 743– 752. MARSHALL, J.J. and RABINOWITZ, M.L. 1976. Preparation and characterization of a dextran-trypsin conjugate. J. Biol. Chem. 251, 1081– 1087. MARUYAMA, S., MITACHI, H., TANAKA, H., TOMIZUKA, N. and ZUZUKI, H. 1987. Studies on the active site and antihypertensive activity of angiotensin I converting enzyme inhibitors derived from casein. Agric. Biol. Chem. 51, 1581– 1586. MATHEIS, G. 1991. Phosphorylation of food proteins with phosphorus oxychloride: Improvement of functional and nutritional properties. Food Chem. 39, 13– 26. MATHEIS, G., PENNER, H.M, FEENEY, R.E. and WHITAKER, J.R. 1983. Phosphorylation of casein and lysozyme by phosphorus oxychloride. J. Agric. Food Chem. 31, 379– 387. MATSUDA, T., KATO, Y. and NAKAMURA, R. 1991. Amino carbonyl reaction of ß-lactoglobulin with lactose. J. Agric. Food Chem. 39, 1201– 1204. MATSUDOMI, N., INOUE, Y., NAKASHIMA, H., KATO, A. and KOBAYASHI, K. 1995. Emulsion stabilization by Maillard-type covalent complex of plasma protein with galactomannan. J. Food Sci. 60, 265– 268 and 283. MAUBOIS, J.L. and LÉONIL, J. 1989. Peptides du lait à activité biologique. Lait 69, 245– 269. McKENZIE, H.A. and RALSTON, G.B. 1971. The denaturation of proteins: two state ? Reversible or irreversible Experientia 27, 617– 744. McKENZIE, H.A., RALSTON, G.B. and SHAW, D.C. 1972. Location of sulfhydryl and disulfide groups in bovine ß-lactoglobulins and effects of urea. Biochemistry 11, 4539– 4547. McKENZIE, H.A. and SAWYER, W.H. 1967. Effect of pH on ß-lactoglobulins. Nature 214, 1101– 1104. MEANS, G.E. and FEENEY, R.E. 1971. Alkylation and similar reagent. Reductive alkylation. In Chemical modification of proteins, 130– 132, Holden-Day Inc., San Francisco . MEDINA, A.L., COLAS, B., LE MESTE, M., RENAUDET, I. and LORIENT, D. 1992. Physicochemical and dynamic properties of caseins modified by chemical phosphorylation. J. Food Sci. 57, 617– 620. MONACO, H.L., ZANOTTI, G., SPADON, P., BOLOGNESI, M., SAWYER, L. and ELIOPOULOS, E.E. 1987. Crystal structure of the trigonal form of bovine ß-lactoglobulin and of its complex with retinol at 2.5 Å resolution. J. Mol. Biol. 197, 695– 706. MONTI, J.C., MERMOUD, A.F. and JOLLÉS, P. 1989. Anti bovine ß-lactoglobulin antibodies react with a human lactoferrin fragment and bovine ß-lactoglobulin present in human milk. Experientia 45, 178– 180. MORGAN, F., LÉONIL, J., MOLLÉ, D. and BOUHALLAB, S. 1997. Nonenzymatic lactosylation of bovine ß-lactoglobulin under mild heat treatment leads to structural heterogeneity of the glycoforms. Biochem. Biophys. Res. Commun. 236, 413– 417. MOTOKI, M. and SEGURO, K. 1998. Transglutaminase and its use for food processing. Trends in Food Sci. and Tech. 9, 204– 210. MYKKANEN, H.M. and WASSERMAN, R.H. 1980. Enhanced absorption of calcium by casein phosphopeptides in rachitic and normal chicks. J. Nutr. 110, 2141– 2148. NACKA, F., CHOBERT, J.M., BUROVA, T., LÉONIL, J. and HAERTLÉ, T. 1998. Induction of new physicochemical and functional properties by the glycation of whey proteins. J. Prot. Chem. 17, 495– 503. NEWCOMER, M.E., JONES, T.A., AQVIST, J., SUNDELIN, J., ERIKSSON, U, RASK, L. and PETERSON, P. 1984. The three dimensional structure of retinol binding protein. EMBO J. 3, 1451– 1454. NONAKA, M., MATSUURA, Y. and MOTOKI, M. 1996. Incorporation of lysine dipeptides into αs1-casein by Ca2+-independent microbial transgluta-minase. Biosci. Biotech. Biochem. 60, 131– 133. NONAKA, M., SAKAMOTO, H., TOIGUCHI, S., KAWAJIRI, H., SOEDA, T. and MOTOKI, M. 1992. Sodium caseinate and skim milk gels formed by incubation with microbial transglutaminase. J. Food Sci. 57, 1214– 1218. NONAKA, M., TANAKA, H., OKIYAMA, A., MOTOKI, M., ANDO, H, UMEDA, K. and MATSUURA, A. 1989. Polymerization of several proteins by Ca2+-independent transglutaminase derived from microorganisms. Agric. Biol. Chem. 53, 2619– 2623. PAPIZ, M.Z., SAWYER, L., ELIOPOULOS, E.E., NORTH, A.L.T., FINDLAY, J.B.C., SIVRAPRASADARAO, R., JONES, T.A., NEWCOMER, M.E. and KRAULIS, P.J. 1986. The structure of ß-lactoglobulin: its similarity to plasma retinol-binding protein. Nature 324, 383– 385. PROVENCHER, S.W. and GLOCKNER, J. 1981. Estimation of globular protein secondary structure from circular dichroism. Biochemistry 20, 33– 37. QI, X.L., BROWNLOW, S, HOLT, C. and SELLER, P. 1995. Thermal denaturation of ß-lactoglobulin: effect of protein concentration at pH 6.75 and 8.05. Biochim. Biophys. Acta 1248, 43– 49. SAEKI, H. 1997. Preparation of neoglycoprotein from carp myofibrillar protein by Maillard reaction with glucose: biochemical properties and emulsifying properties. J. Agric. Food Chem. 45, 680– 684. SAWYER, L. 1967. Heat denaturation of bovine ß-lactoglobulins and relevance of disulfide aggregation. J. Dairy Sci. 51, 323– 329. SHU, Y.W., SAHARA, S, NAKAMURA, S. and KATO, A. 1996. Effects of the length of polysaccharide chains on the functional properties of the Maillard-type lysozyme-polysaccharide conjugate. J. Agric. Food Chem. 44, 2544– 2548. SITOHY, M., CHOBERT, J.M. and HAERTLÉ, T. 1994. Influence of the reaction conditions on the chemical phosphorylation of milk proteins. Milchwissenschaft 49, 610– 615. SITOHY, M., CHOBERT, J.M. and HAERTLÉ, T. 1995a. Phosphorylation of ß-lactoglobulin under mild conditions. J. Agric. Food Chem. 43, 59– 62. SITOHY, M., CHOBERT, J.M. and HAERTLÉ, T. 1995b. Amino acid grafting on ß-lactoglobulin mediated with phosphorus oxychloride. Int. J. Biol. Macromol. 5, 269– 272. SITOHY, M., CHOBERT, J.M, POPINEAU, Y. and HAERTLÉ, T. 1995c. Properties of ß-lactoglobulin phosphorylated in the presence of different aliphatic amines. Lait 75, 503– 512. STAUFF, J., BARTHEL, H., JAENICKE, R., KREKEL, R. and ÜHLEIN, E. 1961. Die Wärmeaggregation von Proteinen in Lösungen. Kolloid Z. 178, 128– 142. SUNG, H.Y., CHEN, H.J, LIU, T. and SU, J.C. 1983. Improvement of functionality of soy protein isolate through chemical phosphorylation. J. Food Sci. 48, 716– 721. SUZUKI, K., MIYOSAWA, Y. and SUZUKI, C. 1963. Protein denaturation by high pressureMeasurements. of turbidity of isoelectrical ovalbumin and horse serum albumin. Arch. Biochem. Biophys. 101, 225– 228. TAINTURIER, G., ROUILLIER, L. and MARTENOT, J.P. 1992. Electroas-sisted glycation of bovine casein: an alternative to the use of reducing chemicals in N-Alkylation of proteins. J. Agric. Food Chem. 40, 760– 763. TANFORD, C. Protein Denaturation. 1968. Adv. Protein Chem. 23, 121– 282. TOWNEND, R., HERSKOVITS, T. and TIMASHEFF, S.N. 1969. The state of amino acid residues in ß-lactoglobulin. Arch. Biochem. Biophys. 129, 567– 580. VAN CAMP, J. and HUYGHEBAERT, A. 1995. High pressure induced gel formation of a whey protein and hemoglobin protein concentrates. European Symposium Effects of high pressure on foods. Montpellier, France. YAYLAYAN, V.A. 1997. Classification of the Maillard reaction: a conceptual approach. Trends in Food Sci. and Tech. 8, 13– 18. YOSHIKAWA, M., SASAKAI, R. and CHIBA, H. 1981. Effect of chemical phosphorylation of bovine casein components on the properties related to casein micelle formation. Agric. Biol. Chem. 45, 909– 914. ZHU, V., RINZEMA, A. and TRAMPER, J. 1995. Microbial transglutaminase. A review of its production and application in food processing. Appl. Microbiol. Biotechnol. 44, 277– 282. Citing Literature Volume23, Issue4October 1999Pages 367-407 ReferencesRelatedInformation" @default.
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• W2122768125 cites W109367216 @default.
• W2122768125 cites W1221193043 @default.
• W2122768125 cites W1492076797 @default.
• W2122768125 cites W1513720422 @default.
• W2122768125 cites W1517875912 @default.
• W2122768125 cites W1541118450 @default.
• W2122768125 cites W1584134504 @default.
• W2122768125 cites W1606860533 @default.
• W2122768125 cites W1653448464 @default.
• W2122768125 cites W1690904680 @default.
• W2122768125 cites W1890457554 @default.
• W2122768125 cites W1966615505 @default.
• W2122768125 cites W1969438039 @default.
• W2122768125 cites W1972594391 @default.
• W2122768125 cites W1980214509 @default.
• W2122768125 cites W1981921408 @default.
• W2122768125 cites W1982461342 @default.
• W2122768125 cites W1982805378 @default.
• W2122768125 cites W1983302383 @default.
• W2122768125 cites W1986216396 @default.
• W2122768125 cites W1986336162 @default.
• W2122768125 cites W1988063719 @default.
• W2122768125 cites W1989507341 @default.
• W2122768125 cites W1991302457 @default.
• W2122768125 cites W1992383396 @default.
• W2122768125 cites W1992975848 @default.
• W2122768125 cites W1994516803 @default.
• W2122768125 cites W1994812138 @default.
• W2122768125 cites W1996100437 @default.
• W2122768125 cites W1996639082 @default.
• W2122768125 cites W1998614995 @default.
• W2122768125 cites W1998624941 @default.
• W2122768125 cites W2001468799 @default.
• W2122768125 cites W2002983560 @default.
• W2122768125 cites W2003742517 @default.
• W2122768125 cites W2004079410 @default.
• W2122768125 cites W2004393198 @default.
• W2122768125 cites W2004974972 @default.
• W2122768125 cites W2007267021 @default.
• W2122768125 cites W2007844422 @default.
• W2122768125 cites W2009985656 @default.
• W2122768125 cites W2010877168 @default.
• W2122768125 cites W2011047428 @default.
• W2122768125 cites W2011770880 @default.
• W2122768125 cites W2014276075 @default.
• W2122768125 cites W2015297175 @default.
• W2122768125 cites W2018229677 @default.
• W2122768125 cites W2020563516 @default.
• W2122768125 cites W2023259031 @default.
• W2122768125 cites W2025402276 @default.
• W2122768125 cites W2028140429 @default.
• W2122768125 cites W2031982331 @default.
• W2122768125 cites W2034891903 @default.
• W2122768125 cites W2036727846 @default.
• W2122768125 cites W2037350922 @default.
• W2122768125 cites W2040056082 @default.
• W2122768125 cites W2041358340 @default.
• W2122768125 cites W2041782866 @default.
• W2122768125 cites W2042670390 @default.
• W2122768125 cites W2042748577 @default.
• W2122768125 cites W2045274336 @default.
• W2122768125 cites W2049955383 @default.
• W2122768125 cites W2050358498 @default.
• W2122768125 cites W2050392278 @default.
• W2122768125 cites W2050894222 @default.
• W2122768125 cites W2051062517 @default.
• W2122768125 cites W2053005758 @default.
• W2122768125 cites W2053023314 @default.
• W2122768125 cites W2054787327 @default.
• W2122768125 cites W2060005665 @default.
• W2122768125 cites W2062985579 @default.
• W2122768125 cites W2064161295 @default.
• W2122768125 cites W2064163209 @default.
• W2122768125 cites W2070133575 @default.
• W2122768125 cites W2070476852 @default.
• W2122768125 cites W2072464742 @default.
• W2122768125 cites W2074947829 @default.
• W2122768125 cites W2075454119 @default.
• W2122768125 cites W2077112638 @default.
• W2122768125 cites W2078946924 @default.
• W2122768125 cites W2079074996 @default.
• W2122768125 cites W2080165605 @default.
• W2122768125 cites W2080314663 @default.
• W2122768125 cites W2083072396 @default.
• W2122768125 cites W2091846020 @default.
• W2122768125 cites W2094077114 @default.
• W2122768125 cites W2094300972 @default.
• W2122768125 cites W2095554353 @default.
• W2122768125 cites W2103265276 @default.
• W2122768125 cites W2111224810 @default.
• W2122768125 cites W2131093311 @default.

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