Protein-flavour interactions

Flavour in Food

Volumn , Issue , 2006, Pages 172-207

  Tromelin, A ^a   Andriot, I ^a   Guichard, E ^a  

^a CENTRE DES SCIENCES DU GOÛT ET DE L ALIMENTATION   (France)

Author keywords

[No Author keywords available]

Indexed keywords

EID: 63749093710     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1533/9781845691400.2.172     Document Type: Chapter

References (207)

1. Adachi M., Takenaka Y., Gidamis A.B., Mikami B., Utsumi S. Crystal structure of soybean proglycinin alaB1b homotrimer. J Mol Biol 2001, 305(2):291-305.
2. Adachi M., Kanamori J., Masuda T., Yagasaki K., Kitamura K., Mikami B., Utsumi S. Crystal structure of soybean 11S globulin: Glycinin A3B4 homohexamer. Proc Natl Acad Sci USA 2003, 100(12):7395-7400.
3. Adams R.L., Mottram D.S., Parker J.K., Brown H.M. Flavor-protein binding: Disulfide interchange reactions between ovalbumin and volatile disulfides. J Agric Food Chem 2001, 49(9):4333-4336.
4. Adler A.J., Greenfield N.J., Fasman G.D. Circular dichroism and optical rotatory dispersion of proteins and polypeptides. Methods Enzymol 1973, 27:675-735.
5. Ahmed M., Dickinson E. Food Polymers, Gels and Colloids. Effects of ethanol on the foaming of food macromolecules 1991, 503-507. The Royal Society of Chemistry, Cambridge. E. Dickinson (Ed.).
6. Akerstrom B., Flower D., Salier J.-S. Lipocalins: unity in diversity. Biochim Biophys Acta 2000, 1482:1-8.
7. Akoh C.C. Fat replacers. Food Technol 1998, 52(3):47-53.
8. Andriot I., Marin I., Feron G., Relkin P., Guichard E. Binding of benzaldehyde by β-lactoglobulin, by static headspace and high performance liquid chromatography in different physico-chemical conditions. Lait 1999, 79(6):577-586.
9. Andriot I., Harrison M., Fournier N., Guichard E. Interactions between methyl ketones and β-lactoglobulin: sensory analysis, headspace analysis, and mathematical modeling. J Agric Food Chem 2000, 48(9):4246-4251.
10. Anema S.G. Effect of milk concentration on the irreversible thermal denaturation and disulfide aggregation of beta-lactoglobulin. J Agric Food Chem 2000, 48:4168-4175.
11. Aouzelleg A., Bull L.A., Price N.C., Kelly S.M. Molecular studies of pressure/temperature-induced structural changes in bovine beta-lactoglobulin. J Sci Food Agric 2004, 84(5):398-404.
12. Aouzelleg A., Bull L.A. Differential scanning calorimetry study of pressure/temperature processed beta-lactoglobulin: The effect of dextran sulphate. Food Res Int 2004, 37(10):933-940.
13. Arrondo Jl R., Muga A., Castresana J., Goni F.M. Quantitative Studies of the Structure of Proteins in Solution by Fourier-Transform Infrared-Spectroscopy. Prog Biophys Mol Biol 1993, 59(1):23-56.
14. Batt C.A., Brady J., Sawyer L. Design improvements of beta-lactoglobulin. Trends Food Sci Technol 1994, 5(8):261-265.
15. Baussay K., Le Bon C., Nicolai T., Durand D., Busnel J.P. Influence of the ionic strength on the heat-induced aggregation of the globular protein beta-lactoglobulin at pH 7. Int J Biol Macromol 2004, 34(1-2):21-28.
16. Belloque J., Lopez-Fandino R., Smith G.M. A H-NMR study on the effect of high pressures on beta-lactoglobulin. J Agric Food Chem 2000, 48:3906-3912.
17. Bertrand-Harb C., Ivanova I.V., Dalgalarrondo M., Haertle T. Evolution of beta-lactoglobulin and alpha-lactalbumin content during yoghurt fermentation. Int Dairy J 2003, 13(1):39-45.
18. Beyeler M., Solms J. Interaction of flavor model compounds with soy protein and bovine serum albumin. Lebensm Wiss Technol 1974, 7(4):217-219.
19. Boudaud N., Dumont J.P. Interaction between flavor components and beta-lactoglobulin. Flavor-Food Interactions 1996, 633:90-97.
20. Brignon G., Mercier J.C., Ribadeau-Dumas B., Das B.C. Primary structure of bovine kappa paracasein. FEBS Lett 1972, 27(2):301-305.
21. Brignon G., Ribadeau Dumas B., Mercier J.C., Pelissier J.P., Das B.C. Complete amino acid sequence of bovine alphaS2-casein. FEBS Lett 1977, 76(2):274-279.
22. Brownlow S., Morais Cabral J.H., Cooper R., Flower D.R., Yewdall S.J., Polikarpov I., North A.C., Sawyer L. Bovine beta-lactoglobulin at 1.8 A resolution - still an enigmatic lipocalin. Structure 1997, 5(4):481-495.
23. Burova T.V., Grinberg N.V., Golubeva I.A., Mashkevich A.Y., Grinberg V.Y., Tolstoguzov V.B. Flavour release in model bovine serum albumin/pectin/2-octanone systems. Food Hydrocoll 1999, 13(1):7-14.
24. Burova T.V., Grinberg N.V., Grinberg V.Y., Tolstoguzov V.B. Binding of odorants to individual proteins and their mixtures. Effects of protein denaturation and association. A plasticized globule state. Colloid Surface A 2003, 213(2-3):235-244.
25. Carter D.C., Ho J.X. Structure of serum albumin. Adv Protein Chem 1994, 45:153-203.
26. Charles M., Bernal B., Guichard E. 8th Weurman Flavour Research Symposium;. Interactions of beta-lactoglobulin with flavour componds 1996, 433-436. Royal Society of Chemistry, Cambridge. A.J. Taylor, D.S. Mottram (Eds.).
27. Chikenji G., Kikuchi M. What is the role of non-native intermediates of beta-lactoglobulin in protein folding?. Proc Natl Acad Sci USA 2000, 97(26):14273-14277.
28. Cho Y., Batt C.A., Sawyer L. Probing the retinol-binding site of bovine beta-lactoglobulin. J Biol Chem 1994, 269(15):1102-1107.
29. Chobpattana W., Jeon I.J., Smith J.S., Loughin T.M. Mechanisms of interaction between vanillin and milk proteins in model systems. J Food Sci 2002, 67(3):973-977.
30. Chrysina E.D., Brew K., Acharya K.R. Crystal structures of apo- and holobovine alpha-lactalbumin at 2.2-A resolution reveal an effect of calcium on interlobe interactions. J. Biol. Chem 2000, 275(47):37021-37029.
31. Clark D.C., Smith L.J. Influence of alcohol-containing spreading solvents on the secondary structure of proteins: a circular dichroism investigation. J Agric Food Chem 1989, 37(3):627-633.
32. Coates J.B., Medeiros J.S., Thanh V.H., Nielsen N.C. Characterization of the subunits of beta-conglycinin. Arch Biochem Biophys 1985, 243(1):184-194.
33. Colmenarejo G., Alvarezpedraglio A., Lavandera J.L. Cheminformatic models to predict binding affinities to human serum albumin. J Med Chem 2001, 44(25):4370-4378.
34. Croguennec T., Bouhallab S., Molle D., O'kennedy B.T., Mehra R. Stable monomerie intermediate with exposed Cys-119 is formed during heat denaturation of beta-lactoglobulin. Biochem Biophys Res Commun 2003, 301(2):465-471.
35. Croguennec T., Molle D., Mehra R., Bouhallab S. Spectroscopic characterization of heat-induced nonnative beta-lactoglobulin monomers. Protein Sci 2004, 13(5):1340-1346.
36. Croguennec T., O'kennedy B.T., Mehra R. Heat-induced denaturation/aggregation of beta-lactoglobulin A and B: kinetics of the first intermediates formed. Int Dairy J 2004, 14(5):399-409.
37. Damodaran S., Kinsella J.E. Stabilization of proteins by solvents. Effect of pH and anions on the positive copperativivity of 2-nonanone binding to bovine serum albumin. J Biol Chem 1980, 255:8503-8508.
38. Damodaran S., Kinsella J.E. Flavor protein interactions. Binding of carbonyls to bovine serum albumin: thermodynamic and conformational effects. J Agric Food Chem 1980, 28(3):567-571.
39. Damodaran S., Kinsella J.E. Interaction of carbonyls with soy protein: conformational effect. J Agric Food Chem 1981, 29(6):1253-1257.
40. Damodaran S., Kinsella J.E. Interaction of carbonyls with soy protein: thermodynamic effects. J Agric Food Chem 1981, 29(6):1249-1253.
41. Dib R., Chobert J.M., Dalgalarrondo M., Haertlé T. Secondary structure changes and peptic hydrolysis of beta-lactoglobulin induced by diols. Biopolymers 1996, 39(1):23-30.
42. Druaux C., Lubbers S., Charpentier C., Voilley A. Effects of physico-chemical parameters of a model wine on the binding of gamma-decalactone on bovine serum albumin. Food Chem 1995, 53:203-207.
43. Dufour E., Haertlé T. Alcohol-induced changes of beta-lactoglobulin-retinol-binding stoichiometry. Protein Eng 1990, 4(2):185-190.
44. Dufour E., Haertlé T. Binding affinities of beta-ionone and related flavor compounds to beta-lactoglobulin: effects of chemical modifications. J. Agric. Food Chem 1990, 38(8):1691-1695.
45. Dufour E., Roger P., Haertlé T. Binding of Benzo(alpha)pyrene, Ellipticine, and Cis-Parinaric Acid to beta-Lactoglobulin: Influence of Protein Modifications. J Prot Chem 1992, 11(6):645-652.
46. Dumont J.P. Flavour Science and Technology. Flavour-protein interactions: a key to aroma persistence 1987, 143-148. John Wiley, Chichester. M. Martens, G.A. Dalen, H. Russwurm (Eds.).
47. Edwards Pj B., Jameson G.B., Palmano K.P., Creamer L.K. Heat-resistant structural features of bovine beta-lactoglobulin A revealed by NMR H/D exchange observations. Int Dairy J 2002, 12(4):331-344.
48. Fang Y., Dalgleish D.G. Conformation of beta-lactoglobulin studied by FTIR: effect of pH, temperature, and adsorption to the oil-water interface. J Colloid Interface Sci 1997, 196(2):292-298.
49. Farrell JH.M., Wickham E.D., Unruh J.J., Qi P.X., Hoagland P.D. Secondary structural studies of bovine caseins: temperature dependence of [beta]-casein structure as analyzed by circular dichroism and FTIR spectroscopy and correlation with micellization. Food Hydrocoll 2001, 15(4-6):341-354.
50. Farrell H.M., Qi P.X., Wickham E.D., Unruh J.J. Secondary structural studies of bovine caseins: Structure and temperature dependence of beta-casein phosphopeptide (1-25) as analyzed by circular dichroism, FTIR spectroscopy, and analytical ultracentrifugation. J Prot Chem 2002, 21(5):307-321.
51. Farrell H.M., Qi P.X., Brown E.M., Cooke P.H., Tunick M.H., Wickham E.D., Unruh J.J. Molten globule structures in milk proteins: Implications for potential new structure-function relationships. J Dairy Sci 2002, 85(3):459-471.
52. Fasman G.D., Bodenheimer E., Pesce A. Fluorescence studies on poly-alpha-amino acids: models of protein conformation. J Biol Chem 1966, 241(4):916-923.
53. Fischer N., Widder S. How proteins influence food flavor. Food Technol 1997, 51(1):68-70.
54. Flower D. The lipocalin protein family: structure and function. Biochem J 1996, 318:1-14.
55. Flower D. Beyond the superfamily: the lipocalin receptors. Biochim Biophys Acta 2000, 1482:327-336.
56. Flower D., North A., Sansom C. The lipocalin protein family: structural and sequence overview. Biochim Biophys Acta 2000, 1482:9-24.
57. Fogolari F., Ragona L., Zetta L., Romagnoli S., De Kruif K.G., Molinari H. Monomeric bovine β-lactoglobulin adopts a β-barrel fold at pH 2. FEBS Lett 1998, 436(2):149-154.
58. Franzen K.L., Kinsella J.E. Parameters affecting the binding of volatile flavor compounds in model food systems. I. Proteins. J Agric Food Chem 1974, 22(4):675-678.
59. Frapin D., Dufour E., Haertlé T. Probing the fatty acid binding site of beta-lactoglobulins. J Prot Chem 1993, 12(4):443-449.
60. Garcia M.C., Torre M., Marina M.L., Laborda F. Composition and characterization of soyabean and related products. Crit Rev Food Sci Nutr 1997, 37(4):361-391.
61. Garcia M.C., Torre M., Laborda F., Marina M.L. Rapid separation of soybean globulins by reversed-phase high-performance liquid chromatography. J Chromatogr A 1997, 758(1):75-83.
62. Green D.W., Aschaffenburg R., Camerman A., Coppola J.C., Dunnill P., Simmons R.M., Komorowski E.S., Sawyer L., Turner E.M.C., Woods K.F. Structure of bovine [beta]-lactoglobulin at 6A resolution. J Mol Biol 1979, 131(2):375-397.
63. Greenfield N., Fasman G.D. Computed circular dichroism spectra for the evaluation of protein conformation. Biochem 1969, 8(10):4108-4116.
64. Grinberg V.Y., Grinberg N.V., Mashkevich A.Y., Burova T.V., Tolstoguzov V.B. Calorimetric study of interaction of ovalbumin with vanillin. Food Hydrocoll 2002, 16(4):333-343.
65. Grosclaude F., Mahe M.F., Ribadeau-Dumas B. Primary structure of alpha casein and of bovine beta casein. Correction. Eur J Biochem 1973, 40(1):323-324.
66. Guichard E. Interactions between flavor compounds and food ingredients and their influence on flavor perception. Food Rev Int 2002, 18(1):49-70.
67. Guichard E., Etiévant P. Measurement of interactions between polysaccharides and flavour compounds by exclusion size chromatography: advantages and limits. Nahr 1998, 42(6):376-379.
68. Guichard E., Langourieux S. Interactions between Beta-lactoglobulin and flavour compounds. Food Chem 2000, 71:301-308.
69. Guth H., Fritzler R. Binding studies and computer-aided modelling of macromolecule/odorant interactions. Chem Biodiv 2004, 1:2001-2023.
70. Hambling S.G., Mcalpine A.S., Sawyer L. Advanced Dairy Chemistry-1. β-lactoglobulin 1992, Elsevier Applied Science, London. P.F. Fox (Ed.).
71. Hansen A.P., Heinis J.J. Decrease of vanillin flavor perception in the presence of casein and whey proteins. J Dairy Sci 1991, 74(9):2936-2940.
72. Hansen A.P., Heinis J.J. Benzaldehyde, citral, and d-limonene flavor perception in the presence of casein and whey proteins. J Dairy Sci 1992, 75(5):1211-1215.
73. Hansen A.P., Booker D.C. Flavor interactions with caseins and whey proteins. Flavor-Food interactions 1996, 75-89. American Chemical Society, Washington, DC. R.J. McGorrin, J.V. Leland (Eds.).
74. Haque Z.U., Aryana K.J. Volatiles in lowfat cheddar cheese containing commercial fat replacers. Food Sci Technol Research 2002, 8(2):188-190.
75. Harrison M., Hills B.P. Mathematical model of flavor release from liquids containing aroma-binding macromolecules. J Agric Food Chem 1997, 45(5):1883-1890.
76. Havea P., Singh H., Creamer L.K. Characterization of heat-induced aggregates of beta-lactoglobulin, alpha-lactalbumin and bovine serum albumin in a whey protein concentrate environment. J Dairy Res 2001, 68(3):483-497.
77. Heng L., Van Koningsveld G.A., Gruppen H., Van Boekel M., Vincken J.P., Roozen J.P., Voragen A.G.J. Protein-flavour interactions in relation to development of novel protein foods. Trends Food Sci Technol 2004, 15(3-4):217-224.
78. Hirayama K., Akashi S., Furuya M., Fukuhara K. Rapid confirmation and revision of the primary structure of bovine serum albumin by ESIMS and Frit-FAB LC/MS. Biochem Biophys Res Commun 1990, 173(2):639-646.
79. Hodgkin D.C. X-ray analysis and protein structure. Cold Spring Harb Symp Quant Biol 1950, 14:65-78.
80. Hoffman M A.M., Van Mil P. Heat-induced aggregation of b-lactoglobulin: role of the free thiol group and disulfide bonds. J Agric Food Chem 1997, 45:2942-2948.
81. Hong Y.H., Creamer L.K. Changed protein structures of bovine beta-lactoglobulin B and alpha-lactalbumin as a consequence of heat treatment. Int Dairy J 2002, 12(4):345-359.
82. Hosseini-Nia T., Ismail A.A., Kubow S. Pressure-induced conformational changes of beta-lactoglobulin by variable-pressure Fourier transform infrared spectroscopy. J Agric Food Chem 1999, 47:4537-4542.
83. Huppertz T., Fox P.F., Kelly A.L. High pressure-induced denaturation of alpha-lactalbumin and beta-lactoglobulin in bovine milk and whey: a possible mechanism. J Dairy Res 2004, 71(4):489-495.
84. Iametti S., Transidico P., Bonomi F., Vecchio G., Pittia P., Rovere P.G.D.A. Molecular modifications of beta-lactoglobulin upon exposure to high pressure. J Agric Food Chem 1997, 45:23-29.
85. Jameson G.B., Adams J.J., Creamer L.K. Flexibility, functionality and hydrophobicity of bovine beta-lactoglobulin. Int Dairy J 2002, 12(4):319-329.
86. Jasinski E., Kilara A. Flavor binding by whey proteins. Milchwissenschaft 1985, 40(10):596-599.
87. Joss L.A., Ralston G.B. Beta-lactoglobulin B: a proposed standard for the study of reversible self-association reactions in the analytical ultracentrifuge?. Anal Biochem 1996, 236(1):20-26.
88. Jouenne E. Etude des interactions entre la beta-lactoglobuline et les composés d'arôme 1997, Thèse de Doctorat, Université de Montpellier 2, France.
89. Jouenne E., Crouzet J., Schieberle P. Measurement of affinity constants by DCCLC. Interaction of Food Matrix with Small Ligands Influencing Flavour and Texture 1997, 68-71. Vol. 3, European Communities. P. Schieberle (Ed.).
90. Jouenne E., Crouzet J. Effect of pH on retention of aroma compounds by b-lactoglobulin. J Agric Food Chem 2000, 48(4):1273-1277.
91. Jung D.-M., Ebeler S.E. Investigation of binding behavior of alpha- and beta-ionones to beta-lactoglobulin at different pH values using a diffusion-based NOE pumping technique. J Agric Food Chem 2003, 51:1988-1993.
92. Jung D.M., De Ropp J.S., Ebeler S.E. Study of interactions between food phenolics and aromatic flavors using one- and two-dimensional H-1 NMR spectroscopy. J Agric Food Chem 2000, 48(2):407-412.
93. Jung D.-A., De Ropp J.S., Ebeler S.E. Application of Pulsed Field Gradient NMR Techniques for Investigating Binding of Flavor Compounds to Macromolecules. J Agric Food Chem 2002, 50(15):4262-4269.
94. Karasova L., Fukal L., Kodicek M., Rauch P. Heat Denaturation of alpha-lactalbumin and beta-lactoglobulin. Chem Pap-Chem Zvesti 1998, 52:552-553.
95. King B.M., Solms J. Sensory Quality in Foods and Beverages: Definition, Measurement and Control. Headspace gas-chromatography as a means of assessing the effect of non-volatile food components on volatile flavour compounds 1983, 196-202. Ellis Horwood, Chichester. A.A. Williams, R.K. Atkin (Eds.).
96. Kinsella J.E. Flavor perception and binding. Inform 1990, 1(3):215.
97. Kister A.E., Finkelstein A.V., Gelfand I.M. Common features in structures and sequences of sandwich-like proteins. Proc Natl Acad Sci USA 2002, 99(22):14137-14141.
98. Ko T.P., Ng J.D., Mcpherson A. The 3-Dimensional Structure of Canavalin from Jack-Bean (Canavalia-Ensiformis). Plant Physiol 1993, 101(3):729-744.
99. Ko T.P., Day J., Mcpherson A. The refined structure of canavalin from jack bean in two crystal forms at 2.1 and 2.0 A resolution. Acta Crystallogr D Biol Crystallogr 2000, 56(Pt 4):411-420.
100. Kontopidis G., Holt C., Sawyer L. The ligand-binding site of bovine beta-lactoglobulin: Evidence for a function?. J Mol Biol 2002, 318(4):1043-1055.
101. Kumosinski T.F., Brown E.M., Farrell H.M. Three-dimensional molecular modeling of bovine caseins: alpha s1-casein. J Dairy Sci 1991, 74(9):2889-2895.
102. Kumosinski T.F., Brown E.M., Farrell H.M. Three-dimensional molecular modeling of bovine caseins: kappa-casein. J Dairy Sci 1991, 74(9):2879-2887.
103. Kumosinski T.F., Brown E.M., Farrell H.M. Three-dimensional molecular modeling of bovine caseins: an energy-minimized beta-casein structure. J Dairy Sci 1993, 76(4):931-945.
104. Kumosinski T.F., Brown E.M., Farrell H.M. Three-dimensional molecular modeling of bovine caseins: a refined, energy-minimized kappa-casein structure. J Dairy Sci 1993, 76(9):2507-2520.
105. Kuwata K., Hoshino M., Forge V., Era S., Batt C.A., Goto Y. Solution structure and dynamics of bovine beta-lactoglobulin A. Protein Sci 1999, 8(11):2541-2545.
106. Labouré H., Cases E., Cayot P. Heat induced beta-lactoglobulin polymerization: role of the change in medium permittivity. Food Chem 2004, 85(3):399-406.
107. Langourieux S. Aroma compound-matrix interactions by dynamic coupled column liquid chromatography. In. Interaction of Food Matrix with Small Ligands Influencing Flavour and Texture 1995, 71-75.
108. Lawrence M.C., Suzuki E., Varghese J.N., Davis P.C., Van Donkelaar A., Tulloch P.A., Colman P.M. The three-dimensional structure of the seed storage protein phaseolin at 3 A resolution. Embo J 1990, 9(1):9-15.
109. Lawrence M.C., Izard T., Beuchat M., Blagrove R.J., Colman P.M. Structure of phaseolin at 2.2 A resolution. Implications for a common vicilin/legumin structure and the genetic engineering of seed storage proteins. J Mol Biol 1994, 238(5):748-776.
110. Le Guen S., Vreeker R. Flavour Research at the Dawn of the Twenty-first Century. Interactions between flavour compunds and milk protein under static and dynamic conditions 2003, 182-187. LavoisierTec &Doc, Paris France. J.L. Le Quéré, P. EtiéVant (Eds.).
111. Le Quéré J.L., LÜBke M., Andriot I., Guichard E. 9th Weurman Flavour Research Symposium. Measurement of interaction between aroma compounds and the protein β-lactoglobulin by spectroscopic methods 1999, 329-333. Deutsche Forschungsanstalt für Lebensmittelchemie, Garching, Germany. P. Schieberle, K.H. Engel (Eds.).
112. Lefèvre T., Subirade M. Structural and interaction properties of beta-lactoglobulin as studied by FTIR spectroscopy. Int J Food Sci Technol 1999, 34:419-428.
113. Liu J.Q., Tian J.N., He W.Y., Xie J.P., Hu Z.D., Chen X.G. Spectrofluorimetric study of the binding of daphnetin to bovine serum albumin. J Pharm Biomed Anal 2004, 35(3):671-677.
114. Lubbers S., Landy P., Voilley A. Retention and release of aroma compounds in foods containing proteins. Food Technol 1998, 52(5):68-74. 208-214.
115. Lübke M., Guichard E., Le Quéré J.L. Flavor Release ACS meeting. Infrared spectroscopic study of β-lactoglobulin interactions with flavour compounds 1999, 282-292. American Chemical Society, Washington, DC. A.J. Taylor, D. Roberts (Eds.).
116. Lübke M., Guichard E., Tromelin A., Le Quéré J.-L. Nuclear magnetic resonance spectroscopic study of beta-lactoglobulin interactions with two flavor compounds, gamma-decalactone and beta-ionone. J Agric Food Chem 2002, 50:7094-7099.
117. Lucca P.A., Tepper B.J. Fat replacers and the functionality of fat in foods. Trends Food Sci Technol 1994, 5(1):12-19.
118. Ma L., Drake M.A., Barbosa Canovas G.V., Swanson B.G. Rheology of full-fat and low-fat Cheddar cheeses as related to type of fat mimetic. J Food Sci 1997, 62(4):748-752.
119. Marabotti A., Balestreri L., Cozzini P., Mozzarelli A., Kellogg G.E., Abraham D.J. HINT predictive analysis of binding between retinol binding protein and hydrophobic ligands. Bioorg Med Chem Lett 2000, 10(18):2129-2132.
120. Marin I. Contribution à l'étude des interactions entre la β-lactoglobuline et certains composés d'arôme. Application à la stabilisation des mousses 1998, Thèse de doctorat, Université Paris XI - Paris Sud, France.
121. Marin I., Relkin P. Foaming properties of beta-lactoglobulin: impact of pre-heating and addition of isoamyl acetate. Int J Food Sci Technol 1999, 34(5/6):517-522.
122. Marin I., Relkin P. Interaction properties of beta-lactoglobulin and benzaldehyde and effect on foaming properties of beta-lactoglobulin. Food Chem 2000, 71:401-406.
123. Maruyama N., Adachi M., Takahashi K., Yagasaki K., Kohno M., Takenaka Y., Okuda E., Nakagawa S., Mikami B., Utsumi S. Crystal structures of recombinant and native soybean beta-conglycinin beta homotrimers. Eur J Biochem 2001, 268(12):3595-3604.
124. Mason K., Patel N.M., Ledel A., Moallemi C.C., Wintner E.A. Mapping protein pockets through their potential small-molecule binding volumes: QSCD applied to biological protein structures. J Comput-Aided Mol Des 2004, 18(1):55-70.
125. May W.E., Wasik S.P., Freeman D.H. Determination of the aqueous solubility of polynuclear aromatic hydrocarbons by a coupled column liquid chromatographic technique. Anal Chem 1978, 50(1):175-179.
126. Mcclements D.J. Modulation of globular protein functionality by weakly interacting cosolvents. Crit Rev Food Sci Nutr 2002, 42(5):417-471.
127. Mcclements D.J., Demetriades K. An integrated approach to the development of reduced-fat food emulsions. Crit Rev Food Sci Nutr 1998, 38(6):511-536.
128. Mcneill V.L., Schmidt K.A. Vanillin interaction with milk protein isolates in sweetened drinks. J Food Sci 1993, 58(5):1142-1147.
129. Mercier J.C., Grosclaude F., Ribadeau-Dumas B. Primary structure of bovine s1 casein. Complete sequence. Eur J Biochem 1971, 23(1):41-51.
130. Mercier J.C., Uro J., Ribadeau-Dumas B., Grosclaude F. Primary structure of a kappa B I bovine casein macropeptide. Eur J Biochem 1972, 27(3):535-547.
131. Meynier A., Rampon V., Dalgalarrondo M., Genot C. Hexanal and t-2-hexenal form covalent bonds with whey proteins and sodium caseinate in aqueous solution. Int Dairy J 2004, 14(8):681-690.
132. Mikheeva L.M., Grinberg N.V., Grinberg V.Y., Tolstoguzov V.B. Effect of thermal denaturation on vanillin binding to some food proteins. Nahr 1998, 42(3/4):185-186.
133. Miles C.A. Differential scanning calorimetry (DSC): protein structure probe useful for the study of damaged tendons. Equine Vet J 1994, 26(4):255-256.
134. Mills O.E., Solms J. Interaction of selected flavour compounds with whey proteins. Lebensm Wiss Technol 1984, 17(6):331-335.
135. Monaco H.L., Zanotti G., Spadon P., Bolognesi M., Sawyer L., Eliopoulos E.E. Crystal structure of the trigonal form of bovine beta-lactoglobulin and of its complex with retinol at 2.5 Å resolution. J Mol Biol 1987, 197:695-706.
136. Morrisett J.D., Pownall H.J., Gotto A.M. Bovine serum albumin. Study of the fatty acid and steroid binding sites using spin-labeled lipids. J Biol Chem 1975, 250(7):2487-2494.
137. Muresan S., Van Der Bent A., De Wolf F.A. Interaction of beta-lactoglobulin with small hydrophobic ligands as monitored by fluorimetry and equilibrium dialysis: Nonlinear quenching effects related to protein-protein association. J Agric Food Chem 2001, 49(5):2609-2618.
138. Narayan M., Berliner L.J. Fatty acids and retinoids bind independently and simultaneously to beta-lactoglobulin. Biochem 1997, 36(7):1906-1911.
139. Nawar W.W. Some considerations in interpretation of direct headspace gas chromatographic analyses of food volatiles. Food Technol 1966, 213(2):115-117.
140. Nawar W.W. Some variables affecting composition of headspace aroma. J Agric Food Chem 1971, 19(6):1057-1059.
141. Ng Pk W., Hoehn E., Bushuk W. Binding of vanillin by fababean proteins. J Food Sci 1989, 54(1):105-107.
142. Ngarize S., Herman H., Adams A., Howell N. Comparison of changes in the secondary structure of unhealed, heated, and high-pressure-treated β-lactoglobulin and ovalbumin proteins using Fourier transform Raman spectroscopy and self-deconvolution. J Agric Food Chem 2004, 52(21):6470-6477.
143. Nielsen N.C., Dickinson C.D., Cho T.J., Thanh V.H., Scallon B.J., Fischer R.L., Sims T.L., Drews G.N., Goldberg R.B. Characterization of the glycinin gene family in soybean. Plant Cell 1989, 1(3):313-328.
144. Nonaka M., Li Chan E., Nakai S. Raman spectroscopic study of thermally induced gelation of whey proteins. J Agric Food Chem 1993, 41(8):1176-1181.
145. O'keefe S., Wilson L.A., Resurreccion A.P., Murphy P.A. Determination of the binding of hexanal to soy glycinin and beta-conglycinin in an aqueous model system using a headspace technique. J Agric Food Chem 1991, 39(6):1022-1028.
146. O'neill T.E. Flavor-Food Interactions. Flavor binding by food proteins: An overview 1996, 59-74. American Chemical Society, Washington, DC, Vol. 633. R.J. Mcgorrin, J.V. Leland (Eds.).
147. O'neill T., Kinsella J.E. Flavor protein interactions: characteristics of 2-nonanone binding to isolated soy protein fractions. J Food Sci 1987, 52(1):98-101.
148. O'neill T.E., Kinsella J.E. Effect of heat treatment and modification on conformation and flavor binding by beta-lactoglobulin. J Food Sci 1988, 53(3):906-909.
149. Palmer J.K. Separation of components of aroma concentrates on the basis of functional group and aroma quality. J Agric Food Chem 1973, 21(5):923-925.
150. Papiz M.Z., Sawyer L., Eliopoulos E.E., North A.C.T., Findlay J.B.C., Sivaprasadarao R., Jones T.A., Newcomer M.F., Kraulis P.J. The structure of beta-lactoglobulin and its similarity to plasma retinol-binding protein. Nature 1986, 324:383-385.
151. Parker J.K., Mottram D.S., Adams R.L. Flavour Research at the Dawn of the Twenty-first Century. Interactions of sulphur-containing aroma compounds with proteins in both model systems and real food systems 2003, 45-50. Lavoisier Tec &Doc, Paris, France. J.L. Le Quéré, P. EtiÉVant (Eds.).
152. Pelletier E., Sostmann K., Guichard E. Measurement of interactions between beta-lactoglobulin and flavor compounds (esters, acids, and pyrazines) by affinity and exclusion size chromatography. J Agric Food Chem 1998, 46(4):1506-1509.
153. Permyakov E.A., Berliner L.J. Alpha-lactalbumin: structure and function. FEBS Lett 2000, 473(3):269-274.
154. Perola E., Charifson P.S. Conformational analysis of drug-like molecules bound to proteins: An extensive study of ligand reorganization upon binding. J Med Chem 2004, 47(10):2499-2510.
155. Phillips L.G., Schulman W., Kinsella J.E. pH and heat treatment effects on foaming of whey protein isolate. J Food Sci 1990, 55(4):1116-1119.
156. Pittia P., Wilde P.J., Husband F.A., Clark D.C. Functional and structural properties of β-lactoglobulin as affected by high pressure treatment. J Food Sci 1996, 61:1123-1128.
157. Plug H., Haring P. The influence of flavour-ingredient interactions on flavour perception. Food Qual Prefer 1994, 5(1/2):95-102.
158. Pouzot M., Durand D., Nicolai T. Influence of the ionic strength on the structure of heat-set globular protein gels at pH 7 beta-lactoglobulin. Macromol 2004, 37(23):8703-8708.
159. Prabakaran S., Damodaran S. Thermal unfolding of beta-lactoglobulin: Characterization of initial unfolding events responsible for heat-induced aggregation. J Agric Food Chem 1997, 45(11):4303-4308.
160. Qi X.L., Holt C., Mcnulty D., Clarke D.T., Brownlow S., Jones G.R. Effect of temperature on the secondary structure of beta-lactoglobulin at pH 6.7, as determined by CD and IR spectroscopy: a test of the molten globule hypothesis. Biochem J 1997, 324:341-346.
161. Qi P.X., Brown E.M., Farrell H.M. "New views" on structure-function relationships in milk proteins. Trends Food Sci Technol 2001, 12(9):339-346.
162. Qi P.X., Unruh J.J., Wickham E.D., Farrell H.M. Structure of bovine beta-casein studied by Fourier-transform infrared spectroscopy and computer modeling. Biophys J 2001, 80(1):399a-398.
163. Qin B.Y., Creamer L.K., Baker E.N., Jameson G.B. 12-Bromododecanoic acid binds inside the calyx of bovine [beta]-lactoglobulin. FEBS Lett 1998, 438(3):272-278.
164. Ragona L., Fogolari F., Zetta L., Perez D.M., Puyol P., De Kruif K., Löhr F., RÜTerjans H., Molinari H. Bovine β-lactoglobulin: Interaction studies with palmitic acid. Prot Sci 2000, 9(7):1347-1356.
165. Refsgaard H.H., Tsai L., Stadtman E.R. Modifications of proteins by polyunsaturated fatty acid peroxidation products. Proc Natl Acad Sci USA 2000, 97(2):611-616.
166. Reiners J., Nicklaus S., Guichard E. Interactions between β-lactoglobulin and flavour compounds of different chemical classes. Impact of the protein on the odour perception of vanillin and eugenol. Lait 2000, 80:347-360.
167. Relkin P., Vermersch J. Food Colloids. Binding properties of vanillin to whey proteins: effects on protein conformational stability and foaming properties 2001, 282-292. Royal Society of Chemistry, Cambridge. E. Dickinson, R. Miller (Eds.).
168. Ribadeau Dumas B., Brignon G., Grosclaude F., Mercier J.C. Primary Structure of bovine beta casein. Complete sequence. Eur J Biochem 1972, 25(3):505-514.
169. Robbins G.A., Wang S., Stuart J.D. Using the static headspace method to determine Henry's law constants. Anal Chem 1993, 65:3113-3118.
170. Sakurai K., Oobatake M., Goto Y. Salt-dependent monomer-dimer equilibrium of bovine beta-lactoglobulin at pH 3. Protein Sci 2001, 10(11):2325-2335.
171. Saleeb F.Z., Pickup J.G. Flavor of Foods and Beverages. Flavor interactions with food ingredients from head-space analysis measurements 1978, 113-130. Academic Press, New York, USA. G. Charalambous, G.E. Inglett (Eds.).
172. Sawyer L., Brownlow S., Polikarpov I., Wu S.Y. Beta-lactoglobulin: structural studies, biological clues. Int Dairy J 1998, 8:65-72.
173. Sawyer L., Kontopidis G. The core lipocalin, bovine beta-lactoglobulin. Bioch Biophys Acta 2000, 1482:136-148.
174. Schmitt S., Kuhn D., Klebe G. A new method to detect related function among proteins independent of sequence and fold homology. J Mol Biol 2002, 323(2):387-406.
175. Semenova M.G., Antipova A.S., Misharina T.A., Golovnya R.V. Binding of aroma compounds with legumin. I. Binding of hexyl acetate with 11S globulin depending on the protein molecular state in aqueous medium. Food Hydrocoll 2002, 16(6):557-564.
176. Semenova M.G., Antipova A.S., Wasserman L.A., Misharina T.A., Golovny A.R.V. Binding of aroma compounds with legumin. II. Effect of hexyl acetate on thermodynamic properties of 11S globulin in aqueous medium. Food Hydrocoll 2002, 16(6):565-571.
177. Semenova M.G., Antipova A.S., Belyakova L.E., Polikarpov Y.N., Wasserman L.A., Misharina T.A., Terenina M.B., Golovnya R.V. Binding of aroma compounds with legumin. III. Thermodynamics of competitive binding of aroma compounds with 11S globulin depending on the structure of aroma compounds. Food Hydrocoll 2002, 16(6):573-584.
178. Seuvre A.M., Diaz M.A.E., Voilley A. Retention of aroma compounds by beta-lactoglobulin in different conditions. Food Chem 2001, 77(4):421-429.
179. Shutov A.D., Kakhovskaya I.A., Braun H., Baumlein H., Muntz K. Legumin-like and vicilin-like seed storage proteins: Evidence for a common single-domain ancestral gene. J Mol Evol 1995, 41(6):1057-1069.
180. Solms J., Guggenbuehl B. Flavour Science and Technology. physical aspects of flavor applications in food systems 1991, Wiley, Chichester, 319-335.
181. Sostmann K., Bernal B., Andriot I., Guichard E. Flavor Perception. Aroma Evaluation. Flavour binding by β-lactoglobulin: different approaches 1997, 425-434. Eigenverlag Universität Postdam, Eisenach. H.-P. Kruse, M. Rothe (Eds.).
182. Sostmann K., Guichard E. Immobilized beta-lactoglobulin on a HPLC-column: a rapid way to determine protein-flavour interactions. Food Chem 1998, 62:509-513.
183. Spector A.A. Fatty acid binding to plasma albumin. J Lipid Res 1975, 16(3):165-179.
184. Stevenson R.J., Chen X.D., Mills O.E. Modern analyses and binding studies of flavour volatiles with particular reference to dairy protein products. Food Res Int 1996, 29(3-4):265-290.
185. Subirade M., Loupil F., Allain A.-F., Paquin P. Effect of dynamic high pressure on the secondary structure of beta-lactoglobulin and on its conformational properties as determined by Fourier transform infrared spectroscopy. Int Dairy J 1998, 8(2):135-140.
186. Surewicz W.K., Mantsch H.H., Chapman D. Determination of protein secondary structure by fourier-transform infrared-spectroscopy - a critical assessment. Biochem 1993, 32(2):389-394.
187. Surroca Y., Haverkamp J., Heck A.J.R. Towards the understanding of molecular mechanisms in the early stages of heat-induced aggregation of beta-lactoglobulin AB. J Chromatogr A 2002, 970(1-2):275-285.
188. Swaisgood H.E. Review and update of casein chemistry. J Dairy Sci 1993, 76(10):3054-3061.
189. Teale F.W. The ultraviolet fluorescence of proteins in neutral solution. Biochem J 1960, 76:381-388.
190. Tian J.N., Liu J.Q., He W.Y., Hu Z.D., Yao X.J., Chen X.G. Probing the binding of scutellarin to human serum albumin by circular dichroism, fluorescence spectroscopy, FTIR, and molecular modeling method. Biomacromol 2004, 5(5):1956-1961.
191. Tromelin A., Guichard E. Use of catalyst in a 3D-QSAR study of the interactions between flavor compounds and β-lactoglobulin. J Agric Food Chem 2003, 51(7):1977-1983.
192. Tromelin A., Guichard E. 2D-and 3D-QSAR models of interaction between flavor compounds and beta-lactoglobulin using catalyst and Cerius2. QSAR Comb Sci 2004, 23(4):214-233.
193. Troy D.J., Desmond E.M., Buckley D.J. Eating quality of low-fat beefburgers containing fat-replacing functional blends. J Sci Food Agric 1999, 79(4):507-516.
194. Tumer N.E., Thanh V.H., Nielsen N.C. Purification and characterization of mRNA from soybean seeds. Identification of glycinin and beta-conglycinin precursors. J Biol Chem 1981, 256(16):8756-8760.
195. Uhrinova S., Uhrin D., Denton H., Smith M., Sawyer L., Barlow P.N. Complete assignment of 1H, 13C and 15N chemical shifts for bovine beta-lactoglobulin: Secondary structure and topology of the native state is retained in a partially unfolded form. J Biomol NMR 1998, 12:89-107.
196. Uhrinova S., Smith M.H., Jameson G.B., Uhrin D., Sawyer L., Barlow P.N. Structural Changes Accompanying pH-induced Dissociation of the β-Lactoglobulin Dimer. Biochem 2000, 39(13):3565-3574.
197. Van Ruth S.M., Villeneuve E. Influence of beta-lactoglobulin, pH and presence of other aroma compounds on the air/liquid partition coefficients of 20 aroma compounds varying in functional group and chain length. Food Chem 2002, 79(2):157-164.
198. Wang Q., Allen J.C., Swaisgood H.E. Binding of lipophilic nutrients to beta-lactoglobulin prepared by bioselective adsorption. J Dairy Sci 1999, 82(2):257-264.
199. Weel Kg C., Boelrijk A.E.M., Burger J.J., Claassen N.E., Gruppen H., Voragen A.G.J., Smit G. Effect of whey protein on the in vivo release of aldehydes. J Agric Food Chem 2003, 51(16):4746-4752.
200. Wong Dw S., Camirand W.M., Pavlath A.E. Structures and functionalities of milk proteins. Crit Rev Food Sci Nutr 1996, 36(8):807-844.
201. Wu S.Y., Pérez M.D., Puyol P., Sawyer L. Beta-lactoglobulin binds palmitate within its central cavity. J Biol Chem 1999, 274(1):170-174.
202. Wüthrich K. NMR assignments as a basis for structural characterization of denatured states of globular proteins. Curr Opin Struc Biol 1994, 4(1):93-99.
203. Yang J., Dunker A.K., Powers J.R., Clark S., Swanson B.G. Beta-lactoglobulin molten globule induced by high pressure. J Agric Food Chem 2001, 49(7):3236-3243.
204. Yang J., Powers J.R., Clark S., Dunker A.K., Swanson B.G. Hydrophobic probe binding of beta-lactoglobulin in the native and molten globule state induced by high pressure as affected by pH, KlO(3) and N-ethylmaleimide. J Agric Food Chem 2002, 50(18):5207-5214.
205. Yang J., Powers J.R., Clark S., Dunker A.K., Swanson B.G. Ligand and flavor binding functional properties of beta-lactoglobulin in the molten globule state induced by high pressure. J Food Sci 2003, 68(2):444-452.
206. Ye A.Q., Singh H., Oldfield D.J., Anema S. Kinetics of heat-induced association of beta-lactoglobulin and alpha-lactalbumin with milk fat globule membrane in whole milk. Int Dairy J 2004, 14(5):389-398.
207. Zsila F. A new ligand for an old lipocalin: induced circular dichroism spectra reveal binding of bilirubin to bovine beta-lactoglobulin. Febs Lett 2003, 539(1-3):85-90.