메뉴 건너뛰기




Volumn 71, Issue 5, 2006, Pages

Interactions of milk proteins and volatile flavor compounds: Implications in the development of protein foods

Author keywords

Binding constant; Flavor binding; Flavor retention; Heat denaturation; Milk proteins

Indexed keywords


EID: 33746362954     PISSN: 00221147     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1750-3841.2006.00051.x     Document Type: Short Survey
Times cited : (150)

References (163)
  • 1
    • 0034827041 scopus 로고    scopus 로고
    • Flavor-protein binding: Disulfide interchange reactions between ovalbumin and volatile disulfldes
    • Adams RL, Mottram DS, Parker JK, Brown HM. 2001. Flavor-protein binding: disulfide interchange reactions between ovalbumin and volatile disulfldes. J Agric Food Chem 49:4333-6.
    • (2001) J Agric Food Chem , vol.49 , pp. 4333-4336
    • Adams, R.L.1    Mottram, D.S.2    Parker, J.K.3    Brown, H.M.4
  • 2
    • 0009012849 scopus 로고
    • Modification of histidine-residues in bovine serum-albumin by reaction with (e)-2-octenal
    • Alaiz M, Girón J. 1994. Modification of histidine-residues in bovine serum-albumin by reaction with (e)-2-octenal. J Agric Food Chem 42:2094-8.
    • (1994) J Agric Food Chem , vol.42 , pp. 2094-2098
    • Alaiz, M.1    Girón, J.2
  • 3
    • 0033800009 scopus 로고    scopus 로고
    • Interactions between methyl ketones and ß-lactoglobulin: Sensory analysis, headspace analysis, and mathematical modeling
    • Andriot I, Harrison M, Fournier N, Guichard E. 2000. Interactions between methyl ketones and ß-lactoglobulin: sensory analysis, headspace analysis, and mathematical modeling. J Agric Food Chem 48:4246-51.
    • (2000) J Agric Food Chem , vol.48 , pp. 4246-4251
    • Andriot, I.1    Harrison, M.2    Fournier, N.3    Guichard, E.4
  • 4
    • 0000713310 scopus 로고    scopus 로고
    • Binding of benzaldehyde by ß-lactoglobulin, by static headspace and high performance liquid chromatography in different physico-chemical conditions
    • Andriot I, Marin I, Feron G, Relkin P, Guichard E. 1999. Binding of benzaldehyde by ß-lactoglobulin, by static headspace and high performance liquid chromatography in different physico-chemical conditions. Lait 79:577-86.
    • (1999) Lait , vol.79 , pp. 577-586
    • Andriot, I.1    Marin, I.2    Feron, G.3    Relkin, P.4    Guichard, E.5
  • 5
    • 0542418748 scopus 로고
    • Solid-phase microextraction with thermal desorption using fused silica optical fibers
    • Arthur CL, Pawliszyn J. 1990. Solid-phase microextraction with thermal desorption using fused silica optical fibers. Anal Chem 62:2145-8.
    • (1990) Anal Chem , vol.62 , pp. 2145-2148
    • Arthur, C.L.1    Pawliszyn, J.2
  • 7
    • 0001176253 scopus 로고
    • Interaction of flavor model compounds with soy protein and bovine serum albumin
    • Beyeler M, Solms J. 1974. Interaction of flavor model compounds with soy protein and bovine serum albumin. Lebensm-Wiss Technol 7:217-9.
    • (1974) Lebensm-Wiss Technol , vol.7 , pp. 217-219
    • Beyeler, M.1    Solms, J.2
  • 8
    • 28444458402 scopus 로고    scopus 로고
    • Influence of the texture of gelatin gels and pectin gels on strawberry flavour release and perception
    • Boland AB, Delahunty CM, van Ruth SM. 2006. Influence of the texture of gelatin gels and pectin gels on strawberry flavour release and perception. Food Chem 96:452-60.
    • (2006) Food Chem , vol.96 , pp. 452-460
    • Boland, A.B.1    Delahunty, C.M.2    Van Ruth, S.M.3
  • 9
    • 0037433088 scopus 로고    scopus 로고
    • Binding of odorants to individual proteins and their mixtures. Effects of protein denaturation and association. A plasticized globule state
    • Burova TV, Grinberg NV, Grinberg W, Tolstoguzov VB. 2003. Binding of odorants to individual proteins and their mixtures. Effects of protein denaturation and association. A plasticized globule state. Colloids Surf A 213:235-44.
    • (2003) Colloids Surf A , vol.213 , pp. 235-244
    • Burova, T.V.1    Grinberg, N.V.2    Grinberg, W.3    Tolstoguzov, V.B.4
  • 11
    • 0344454771 scopus 로고    scopus 로고
    • The effect of gelling agent type and concentration on flavor release in model systems
    • McGorrin RJ, Leland JV, editors. Washington, D.C.: American Chemical Society
    • Carr J, Baloga D, Guinard JX, Lawter L, Marty C, Squire C. 1996. The effect of gelling agent type and concentration on flavor release in model systems. In: McGorrin RJ, Leland JV, editors. Flavor-food interactions. Washington, D.C.: American Chemical Society. p 98-108.
    • (1996) Flavor-Food Interactions , pp. 98-108
    • Carr, J.1    Baloga, D.2    Guinard, J.X.3    Lawter, L.4    Marty, C.5    Squire, C.6
  • 12
    • 0002142681 scopus 로고    scopus 로고
    • Interaction of ß-lactoglobulin with flavour compounds
    • Taylor AJ, Mottram DS, editors. Cambridge, U.K.: Royal Society of Chemistry
    • Charles M, Bernal B, Guichard E. 1996. Interaction of ß-lactoglobulin with flavour compounds. In: Taylor AJ, Mottram DS, editors. Flavour science: recent developments. Cambridge, U.K.: Royal Society of Chemistry. p 433-6.
    • (1996) Flavour Science: Recent Developments , pp. 433-436
    • Charles, M.1    Bernal, B.2    Guichard, E.3
  • 13
    • 0036262797 scopus 로고    scopus 로고
    • Mechanisms of interaction between vanillin and milk proteins in model systems
    • Chobpattana W, Jeon IJ, Smith JS, Loughin TM. 2002. Mechanisms of interaction between vanillin and milk proteins in model systems. J Food Sci 67:973-7.
    • (2002) J Food Sci , vol.67 , pp. 973-977
    • Chobpattana, W.1    Jeon, I.J.2    Smith, J.S.3    Loughin, T.M.4
  • 14
    • 0000338743 scopus 로고    scopus 로고
    • A study of the behavior of Maillard reaction products analyzed by solid-phase microextraction gas chromatography mass selective detection
    • Coleman WM. 1996. A study of the behavior of Maillard reaction products analyzed by solid-phase microextraction gas chromatography mass selective detection. J Chromatogr Sci 34:213-8.
    • (1996) J Chromatogr Sci , vol.34 , pp. 213-218
    • Coleman, W.M.1
  • 15
    • 17144407576 scopus 로고    scopus 로고
    • Influence of binding of sodium dodecyl sulfate, all-trans-retinol, palmitate, and 8-anilino-1-naphthalenesulfonate on the heat-induced unfolding and aggregation of ß-lactoglobulin B
    • Considine T, Patel HA, Singh H, Creamer LK. 2005a. Influence of binding of sodium dodecyl sulfate, all-trans-retinol, palmitate, and 8-anilino-1-naphthalenesulfonate on the heat-induced unfolding and aggregation of ß-lactoglobulin B. J Agric Food Chem 53:3197-205.
    • (2005) J Agric Food Chem , vol.53 , pp. 3197-3205
    • Considine, T.1    Patel, H.A.2    Singh, H.3    Creamer, L.K.4
  • 16
    • 27144526439 scopus 로고    scopus 로고
    • Influence of binding of sodium dodecyl sulfate, all-trans-retinol, and 8-anilino-1-naphthalenesulfonate on the high-pressure-induced unfolding and aggregation of ß-lactoglobulin B
    • Considine T, Singh H, Patel HA, Creamer LK. 2005b. Influence of binding of sodium dodecyl sulfate, all-trans-retinol, and 8-anilino-1- naphthalenesulfonate on the high-pressure-induced unfolding and aggregation of ß-lactoglobulin B. J Agric Food Chem 53:8010-8.
    • (2005) J Agric Food Chem , vol.53 , pp. 8010-8018
    • Considine, T.1    Singh, H.2    Patel, H.A.3    Creamer, L.K.4
  • 17
    • 0019332927 scopus 로고
    • Stabilization of proteins by solvents-effect of pH and anions on the positive cooperativity of 2-nonanone binding to bovine serum albumin
    • Damodaran S, Kinsella JE. 1980a. Stabilization of proteins by solvents-effect of pH and anions on the positive cooperativity of 2-nonanone binding to bovine serum albumin. J Biol Chem 255:8503-8.
    • (1980) J Biol Chem , vol.255 , pp. 8503-8508
    • Damodaran, S.1    Kinsella, J.E.2
  • 18
    • 0019016883 scopus 로고
    • Flavor protein interactions-binding of carbonyls to bovine serum albumin-thermodynamic and conformational effects
    • Damodaran S, Kinsella JE. 1980b. Flavor protein interactions-binding of carbonyls to bovine serum albumin-thermodynamic and conformational effects. J Agric Food Chem 28:567-71.
    • (1980) J Agric Food Chem , vol.28 , pp. 567-571
    • Damodaran, S.1    Kinsella, J.E.2
  • 19
    • 0000642766 scopus 로고
    • Interaction of carbonyls with soy protein-thermodynamic effects
    • Damodaran S, Kinsella JE. 1981a. Interaction of carbonyls with soy protein-thermodynamic effects. J Agric Food Chem 29:1249-53.
    • (1981) J Agric Food Chem , vol.29 , pp. 1249-1253
    • Damodaran, S.1    Kinsella, J.E.2
  • 20
    • 33845556477 scopus 로고
    • Interaction of carbonyls with soy protein-conformational effects
    • Damodaran S, Kinsella JE. 1981b. Interaction of carbonyls with soy protein-conformational effects. J Agric Food Chem 29:1253-7.
    • (1981) J Agric Food Chem , vol.29 , pp. 1253-1257
    • Damodaran, S.1    Kinsella, J.E.2
  • 21
    • 0019519117 scopus 로고
    • The effects of neutral salts on the stability of macromolecules - A new approach using a protein-ligand binding system
    • Damodaran S, Kinsella JE. 1981c. The effects of neutral salts on the stability of macromolecules-a new approach using a protein-ligand binding system. J Biol Chem 256:3394-8.
    • (1981) J Biol Chem , vol.256 , pp. 3394-3398
    • Damodaran, S.1    Kinsella, J.E.2
  • 22
    • 0012814277 scopus 로고
    • Binding of carbonyls to fish actomyosin
    • Damodaran S, Kinsella JE. 1983. Binding of carbonyls to fish actomyosin. J Agric Food Chem 31:856-9.
    • (1983) J Agric Food Chem , vol.31 , pp. 856-859
    • Damodaran, S.1    Kinsella, J.E.2
  • 23
    • 0002864325 scopus 로고
    • Structure and functional behaviour of whey proteins
    • de Wit JN. 1981. Structure and functional behaviour of whey proteins. Neth Milk Dairy J 35:47-64.
    • (1981) Neth Milk Dairy J , vol.35 , pp. 47-64
    • De Wit, J.N.1
  • 25
    • 33644969406 scopus 로고    scopus 로고
    • Investigation of the retronasal flavour release during the consumption of coffee with additions of milk constituents by Oral breath sampling
    • Denker M, Parat-Wilhelms M, Drichelt G, Paucke J, Luger A, Borcherding K, Hoffmann W, Steinhart H. 2006. Investigation of the retronasal flavour release during the consumption of coffee with additions of milk constituents by Oral breath sampling. Food Chem 98:201-8.
    • (2006) Food Chem , vol.98 , pp. 201-208
    • Denker, M.1    Parat-Wilhelms, M.2    Drichelt, G.3    Paucke, J.4    Luger, A.5    Borcherding, K.6    Hoffmann, W.7    Steinhart, H.8
  • 26
    • 33746338137 scopus 로고
    • Reaction of vanillin with albumin
    • Maarse H, Groenen PJ, editors. Wageningen: Pudoc
    • Dhont JH. 1987. Reaction of vanillin with albumin. In: Maarse H, Groenen PJ, editors. Aroma research. Wageningen: Pudoc. p 193-4.
    • (1987) Aroma Research , pp. 193-194
    • Dhont, J.H.1
  • 28
    • 0028908116 scopus 로고
    • Effects of physicochemical parameters of a model wine on the binding of γ-decalactone on bovine serum albumin
    • Druaux C, Lubbers S, Charpentier C, Voilley A. 1995. Effects of physicochemical parameters of a model wine on the binding of γ-decalactone on bovine serum albumin. Food Chem 53:203-7.
    • (1995) Food Chem , vol.53 , pp. 203-207
    • Druaux, C.1    Lubbers, S.2    Charpentier, C.3    Voilley, A.4
  • 29
    • 1542577682 scopus 로고    scopus 로고
    • Flavoring of complex media: A model cheese example
    • McGorrin RJ, Leland JV, editors. Washington, D.C.: American Chemical Society
    • Dubois C, Sergent M, Voilley A. 1996. Flavoring of complex media: a model cheese example. In: McGorrin RJ, Leland JV, editors. Flavor-food interactions. Washington, D.C.: American Chemical Society. p 217-26.
    • (1996) Flavor-food Interactions , pp. 217-226
    • Dubois, C.1    Sergent, M.2    Voilley, A.3
  • 30
    • 0001510699 scopus 로고
    • Binding affinities of ß-ionone and related flavor compounds to ß-lactoglobulin-effects of chemical modifications
    • Dufour E, Haertlé T. 1990. Binding affinities of ß-ionone and related flavor compounds to ß-lactoglobulin-effects of chemical modifications. J Agric Food Chem 38:1691-5.
    • (1990) J Agric Food Chem , vol.38 , pp. 1691-1695
    • Dufour, E.1    Haertlé, T.2
  • 31
    • 0343067720 scopus 로고
    • Flavour-protein interactions: A key to aroma persistence
    • Martens M, Dalen GA, Russwurm H, editors. Chichester: John Wiley and Sons
    • Dumont JP. 1987. Flavour-protein interactions: a key to aroma persistence. In: Martens M, Dalen GA, Russwurm H, editors. Flavour science and technology. Chichester: John Wiley and Sons. p 143-8.
    • (1987) Flavour Science and Technology , pp. 143-148
    • Dumont, J.P.1
  • 32
    • 0001247035 scopus 로고
    • Binding of diacetyl by pea proteins
    • Dumont JP, Land DG. 1986. Binding of diacetyl by pea proteins. J Agric Food Chem 34:1041-5.
    • (1986) J Agric Food Chem , vol.34 , pp. 1041-1045
    • Dumont, J.P.1    Land, D.G.2
  • 33
    • 0000048730 scopus 로고
    • Influence of dispersion medium on aroma intensity and headspace concentration of menthone and isoamyl acetate
    • Ebeler SE, Pangborn HM, Jennings WG. 1988. Influence of dispersion medium on aroma intensity and headspace concentration of menthone and isoamyl acetate. J Agric Food Chem 36:791-6.
    • (1988) J Agric Food Chem , vol.36 , pp. 791-796
    • Ebeler, S.E.1    Pangborn, H.M.2    Jennings, W.G.3
  • 34
    • 0037070342 scopus 로고    scopus 로고
    • Comparison of different methods: Static and dynamic headspace and solid-phase microextraction for the measurement of interactions between milk proteins and flavor compounds with an application to emulsions
    • Fabre M, Aubry V, Guichard E. 2002. Comparison of different methods: static and dynamic headspace and solid-phase microextraction for the measurement of interactions between milk proteins and flavor compounds with an application to emulsions. J Agric Food Chem 50:1497-501.
    • (2002) J Agric Food Chem , vol.50 , pp. 1497-1501
    • Fabre, M.1    Aubry, V.2    Guichard, E.3
  • 35
    • 0012871946 scopus 로고    scopus 로고
    • Physicochemical interactions between aroma compounds and milk proteins: Effect of water and protein modification
    • Fares K, Landy P, Guilard R, Voilley A. 1998. Physicochemical interactions between aroma compounds and milk proteins: effect of water and protein modification. J Dairy Sci 81:82-91.
    • (1998) J Dairy Sci , vol.81 , pp. 82-91
    • Fares, K.1    Landy, P.2    Guilard, R.3    Voilley, A.4
  • 36
    • 0002458235 scopus 로고    scopus 로고
    • How proteins influence food flavor
    • Fischer N, Widder S. 1997. How proteins influence food flavor. Food Technol 51:68-70.
    • (1997) Food Technol , vol.51 , pp. 68-70
    • Fischer, N.1    Widder, S.2
  • 37
    • 84974398987 scopus 로고
    • Milk proteins-molecular, colloidal and functional properties
    • Fox PF, Mulvihill DM. 1982. Milk proteins-molecular, colloidal and functional properties. J Dairy Res 49:679-93.
    • (1982) J Dairy Res , vol.49 , pp. 679-693
    • Fox, P.F.1    Mulvihill, D.M.2
  • 38
    • 0000020280 scopus 로고
    • Parameters affecting binding of volatile flavor compounds in model food systems, 1. Proteins
    • Franzen KL, Kinsella JE. 1974. Parameters affecting binding of volatile flavor compounds in model food systems, 1. Proteins. J Agric Food Chem 22:675-8.
    • (1974) J Agric Food Chem , vol.22 , pp. 675-678
    • Franzen, K.L.1    Kinsella, J.E.2
  • 39
    • 0027522088 scopus 로고
    • Probing the fatty-acid-binding site of ß-lactoglobulins
    • Frapin D, Dufour E, Haertlé T. 1993. Probing the fatty-acid-binding site of ß-lactoglobulins. J Prot Chem 12:443-9.
    • (1993) J Prot Chem , vol.12 , pp. 443-449
    • Frapin, D.1    Dufour, E.2    Haertlé, T.3
  • 40
    • 0019331472 scopus 로고
    • Spectroscopic characterization of ß-lactoglobulin-retinol complex
    • Fugate RD, Song PS. 1980. Spectroscopic characterization of ß-lactoglobulin-retinol complex. Biochim Biophys Acta 625:28-42.
    • (1980) Biochim Biophys Acta , vol.625 , pp. 28-42
    • Fugate, R.D.1    Song, P.S.2
  • 41
    • 0015523573 scopus 로고
    • Enhancement of fluorescence and decreased susceptibility to enzymatic oxidation of retinol complexed with bovine serum albumin, ß-lactoglobulin, and the retinol-binding protein of human plasma
    • Futterman S, Heller J. 1972. Enhancement of fluorescence and decreased susceptibility to enzymatic oxidation of retinol complexed with bovine serum albumin, ß-lactoglobulin, and the retinol-binding protein of human plasma. J Biol Chem 247:5168-72.
    • (1972) J Biol Chem , vol.247 , pp. 5168-5172
    • Futterman, S.1    Heller, J.2
  • 42
    • 14644437016 scopus 로고    scopus 로고
    • Interaction of soluble peptides and proteins from skeletal muscle with volatile compounds in model systems as affected by curing agents
    • Gianelli MP, Flores M, Toldra F. 2005. Interaction of soluble peptides and proteins from skeletal muscle with volatile compounds in model systems as affected by curing agents. J Agric Food Chem 53:1670-7.
    • (2005) J Agric Food Chem , vol.53 , pp. 1670-1677
    • Gianelli, M.P.1    Flores, M.2    Toldra, F.3
  • 43
    • 51249189419 scopus 로고
    • Interaction of flavor compounds with soy protein
    • Gremli HA. 1974. Interaction of flavor compounds with soy protein. J Am Oil Chem Soc 51:A95-A97.
    • (1974) J Am Oil Chem Soc , vol.51
    • Gremli, H.A.1
  • 44
    • 0031568680 scopus 로고    scopus 로고
    • Solid-phase microextraction for the analysis of human breath
    • Grote C, Pawliszyn J. 1997. Solid-phase microextraction for the analysis of human breath. Anal Chem 69:587-96.
    • (1997) Anal Chem , vol.69 , pp. 587-596
    • Grote, C.1    Pawliszyn, J.2
  • 45
    • 0034670197 scopus 로고    scopus 로고
    • Interactions between ß-lactoglobulin and flavour compounds
    • Guichard E, Langourieux S. 2000. Interactions between ß-lactoglobulin and flavour compounds. Food Chem 71:301-8.
    • (2000) Food Chem , vol.71 , pp. 301-308
    • Guichard, E.1    Langourieux, S.2
  • 46
    • 33746351961 scopus 로고    scopus 로고
    • Binding studies and computer-aided modelling of macromolecule/odorant interactions
    • Guth H, Fritzler R. 2004. Binding studies and computer-aided modelling of macromolecule/odorant interactions. Chem Biodiv 1:2001-23.
    • (2004) Chem Biodiv , vol.1 , pp. 2001-2023
    • Guth, H.1    Fritzler, R.2
  • 47
    • 1542472678 scopus 로고    scopus 로고
    • Flavor interaction with casein and whey protein
    • McGorrin RJ, Leland JV, editors. Washington, D.C.: American Chemical Society
    • Hansen AP, Booker DC, 1996. Flavor interaction with casein and whey protein. In: McGorrin RJ, Leland JV, editors. Flavor-food interactions. Washington, D.C.: American Chemical Society. p 75-89.
    • (1996) Flavor-food Interactions , pp. 75-89
    • Hansen, A.P.1    Booker, D.C.2
  • 48
    • 0001573152 scopus 로고
    • Decrease of vanillin flavor perception in the presence of casein and whey proteins
    • Hansen AP, Heinis JJ. 1991. Decrease of vanillin flavor perception in the presence of casein and whey proteins. J Dairy Sci 74:2936-40.
    • (1991) J Dairy Sci , vol.74 , pp. 2936-2940
    • Hansen, A.P.1    Heinis, J.J.2
  • 49
    • 0026862449 scopus 로고
    • Benzaldehyde, citral, and d-limonene flavor perception ir the presence of casein and whey proteins
    • Hansen AP, Heinis JJ. 1992. Benzaldehyde, citral, and d-limonene flavor perception ir the presence of casein and whey proteins. J Dairy Sci 75:1211-5.
    • (1992) J Dairy Sci , vol.75 , pp. 1211-1215
    • Hansen, A.P.1    Heinis, J.J.2
  • 50
    • 0002117327 scopus 로고    scopus 로고
    • Implications of fat on flavor
    • McGorrin RJ, Leland JV, editors. Washington, D.C.: American Chemical Society
    • Hatchwell LC. 1996. Implications of fat on flavor. In: McGorrin RJ, Leland JV, editors. Flavor-food interactions. Washington, D.C.: American Chemical Society p 14-23.
    • (1996) Flavor-food Interactions , pp. 14-23
    • Hatchwell, L.C.1
  • 51
    • 0034768130 scopus 로고    scopus 로고
    • Characterization of heat-induced aggregate: Of ß-lactoglobulin, α-lactalbumin and bovine serum albumin in a whey protein concentrate environment
    • Havea P, Singh H, Creamer LK. 2001. Characterization of heat-induced aggregate: of ß-lactoglobulin, α-lactalbumin and bovine serum albumin in a whey protein concentrate environment. J Dairy Res 68:483-97.
    • (2001) J Dairy Res , vol.68 , pp. 483-497
    • Havea, P.1    Singh, H.2    Creamer, L.K.3
  • 52
    • 0026720630 scopus 로고
    • Solventless determination of caffeine in beverages using solid-phase microextraction with fused-silica fibers
    • Hawthorne SB, Miller DJ, Pawliszyn J, Arthur CL. 1992. Solventless determination of caffeine in beverages using solid-phase microextraction with fused-silica fibers. Chrom 603:185-91.
    • (1992) Chrom , vol.603 , pp. 185-191
    • Hawthorne, S.B.1    Miller, D.J.2    Pawliszyn, J.3    Arthur, C.L.4
  • 55
    • 0003043542 scopus 로고
    • The possible effects of the aggregation of the molecules of haemoglobin on its dissociation curves
    • Hill AV. 1910. The possible effects of the aggregation of the molecules of haemoglobin on its dissociation curves. Proc Physiol Soc (London) 40:IV-VII.
    • (1910) Proc Physiol Soc (London) , vol.40
    • Hill, A.V.1
  • 56
    • 50549168907 scopus 로고
    • Measurement of protein-binding phenomena by get filtration
    • Hummel JR, Dreyer WJ. 1962. Measurement of protein-binding phenomena by get filtration. Biochim Biophys Acta 63:530-2.
    • (1962) Biochim Biophys Acta , vol.63 , pp. 530-532
    • Hummel, J.R.1    Dreyer, W.J.2
  • 57
    • 0032539604 scopus 로고    scopus 로고
    • The pressure dependence of hydrophobia interactions is consistent with the observed pressure denaturation of proteins
    • Hummer G, Garde S, Garcia AE, Paulaitis ME, Pratt LR. 1998. The pressure dependence of hydrophobia interactions is consistent with the observed pressure denaturation of proteins. Proc Nat Acad Sci USA 95:1552-5.
    • (1998) Proc Nat Acad Sci USA , vol.95 , pp. 1552-1555
    • Hummer, G.1    Garde, S.2    Garcia, A.E.3    Paulaitis, M.E.4    Pratt, L.R.5
  • 58
    • 1542372830 scopus 로고    scopus 로고
    • High pressure treatment of bovine milk: Effects on casein micelles and whey proteins
    • Huppertz T, Fox PF, Kelly AL. 2004. High pressure treatment of bovine milk: effects on casein micelles and whey proteins. J Dairy Res 71:97-106.
    • (2004) J Dairy Res , vol.71 , pp. 97-106
    • Huppertz, T.1    Fox, P.F.2    Kelly, A.L.3
  • 59
    • 84977730859 scopus 로고
    • A study of texture-flavor interactions using free choice profiling
    • Jaime I, Mela DJ, Bratchell N. 1993. A study of texture-flavor interactions using free choice profiling. J Sens Stud 8:177-88.
    • (1993) J Sens Stud , vol.8 , pp. 177-188
    • Jaime, I.1    Mela, D.J.2    Bratchell, N.3
  • 60
    • 0001575393 scopus 로고
    • Flavor binding by whey proteins
    • Jasinski E, Kilara A. 1985. Flavor binding by whey proteins. Milchwiss 40:596-9.
    • (1985) Milchwiss , vol.40 , pp. 596-599
    • Jasinski, E.1    Kilara, A.2
  • 61
    • 0000564196 scopus 로고    scopus 로고
    • Interaction of aroma compounds with β-lactoglobulin
    • Taylor AJ, Mottram DS, editors. Cambridge, U.K.: Royal Society of Chemistry
    • Jouenne E, Crouzet J. 1996. Interaction of aroma compounds with β-lactoglobulin. In: Taylor AJ, Mottram DS, editors. Flavour science: recent developments. Cambridge, U.K.: Royal Society of Chemistry. p 425-9.
    • (1996) Flavour Science: Recent Developments , pp. 425-429
    • Jouenne, E.1    Crouzet, J.2
  • 62
    • 0033671303 scopus 로고    scopus 로고
    • Determination of apparent binding constants for aroma compounds with β-lactoglobulin by dynamic coupled column liquid chromatography
    • Jouenne E, Crouzet J. 2000a. Determination of apparent binding constants for aroma compounds with β-lactoglobulin by dynamic coupled column liquid chromatography. J Agric Food Chem 48:5396-400.
    • (2000) J Agric Food Chem , vol.48 , pp. 5396-5400
    • Jouenne, E.1    Crouzet, J.2
  • 63
    • 0034055344 scopus 로고    scopus 로고
    • Effect of pH on retention of aroma compounds by β-lactoglobulin
    • Jouenne E, Crouzet J. 2000b. Effect of pH on retention of aroma compounds by β-lactoglobulin. J Agric Food Chem 48:1273-7.
    • (2000) J Agric Food Chem , vol.48 , pp. 1273-1277
    • Jouenne, E.1    Crouzet, J.2
  • 64
    • 0346059509 scopus 로고    scopus 로고
    • Partition coefficients of aroma compounds in polysaccharide solutions by the phase ratio variation method
    • Jouquand C, Ducruet V, Giampaoli P. 2004. Partition coefficients of aroma compounds in polysaccharide solutions by the phase ratio variation method. Food Chem 85:467-74.
    • (2004) Food Chem , vol.85 , pp. 467-474
    • Jouquand, C.1    Ducruet, V.2    Giampaoli, P.3
  • 65
    • 0037227853 scopus 로고    scopus 로고
    • Headspace solid-phase microextraction method for the study of the volatility of selected flavor compounds
    • Jung DM, Ebeler SE. 2003a. Headspace solid-phase microextraction method for the study of the volatility of selected flavor compounds. J Agric Food Chem 51:200-5.
    • (2003) J Agric Food Chem , vol.51 , pp. 200-205
    • Jung, D.M.1    Ebeler, S.E.2
  • 66
    • 0037467420 scopus 로고    scopus 로고
    • Investigation of binding behavior of α- and β-ionones to β-lactoglobulin at different pH values using a diffusion-based NOE pumping technique
    • Jung DM, Ebeler SE. 2003b. Investigation of binding behavior of α- and β-ionones to β-lactoglobulin at different pH values using a diffusion-based NOE pumping technique. J Agric Food Chem 51:1988-93.
    • (2003) J Agric Food Chem , vol.51 , pp. 1988-1993
    • Jung, D.M.1    Ebeler, S.E.2
  • 67
    • 0037125101 scopus 로고    scopus 로고
    • Application of pulsed field gradient NMR techniques for investigating binding of flavor compounds to macromolecules
    • Jung DM, de Ropp JS, Ebeler SE. 2002. Application of pulsed field gradient NMR techniques for investigating binding of flavor compounds to macromolecules. J Agric Food Chem 50:4262-9.
    • (2002) J Agric Food Chem , vol.50 , pp. 4262-4269
    • Jung, D.M.1    De Ropp, J.S.2    Ebeler, S.E.3
  • 68
    • 0001729450 scopus 로고
    • Interactions of flavor compounds in model food systems using benzyl alcohol as an example
    • King BM, Solms J. 1979. Interactions of flavor compounds in model food systems using benzyl alcohol as an example, J Agric Food Chem 27:1331-4.
    • (1979) J Agric Food Chem , vol.27 , pp. 1331-1334
    • King, B.M.1    Solms, J.2
  • 69
    • 0024822645 scopus 로고
    • Proteins in whey: Chemical, physical, and functional properties
    • Kinsella JE, Whitehead DM. 1989. Proteins in whey: chemical, physical, and functional properties. Adv Food Nutr Res 33:343-438.
    • (1989) Adv Food Nutr Res , vol.33 , pp. 343-438
    • Kinsella, J.E.1    Whitehead, D.M.2
  • 70
    • 33746333186 scopus 로고
    • The combination of adenine, adenosine, and adenylic acid with serum albumin
    • Klotz IM, Urquhart JM. 1948. The combination of adenine, adenosine, and adenylic acid with serum albumin. J Biol Chem 173:21-4.
    • (1948) J Biol Chem , vol.173 , pp. 21-24
    • Klotz, I.M.1    Urquhart, J.M.2
  • 71
  • 72
    • 0002703204 scopus 로고    scopus 로고
    • Perspectives on the effects of interactions on flavor perception: An overview
    • McGorrin RJ, Leland JV, editors. Washington, D.C.: American Chemical Society
    • Land DG. 1996. Perspectives on the effects of interactions on flavor perception: an overview. In: McGorrin RJ, Leland JV, editors. Flavor-food Interactions. Washington, D.C.: American Chemical Society, p 2-11.
    • (1996) Flavor-food Interactions , pp. 2-11
    • Land, D.G.1
  • 73
    • 0002921312 scopus 로고
    • The influence of food components on the volatility of diacetyl
    • Schreier P, editor. Berlin: Walter de Gruyter
    • Land DG, Reynolds J. 1981. The influence of food components on the volatility of diacetyl. In: Schreier P, editor. Flavour '81. Berlin: Walter de Gruyter. p 701-5.
    • (1981) Flavour '81 , pp. 701-705
    • Land, D.G.1    Reynolds, J.2
  • 74
    • 0028829088 scopus 로고
    • Retention of aroma compounds by proteins in aqueous solution
    • Landy P, Druaux C, Voilley A. 1995. Retention of aroma compounds by proteins in aqueous solution. Food Chem 54:387-92.
    • (1995) Food Chem , vol.54 , pp. 387-392
    • Landy, P.1    Druaux, C.2    Voilley, A.3
  • 75
    • 0009259476 scopus 로고    scopus 로고
    • Effect of chemical modification of sodium caseinate on diffusivity of aroma compounds in aqueous solutions
    • Landy P, Fares K, Lorient D, Voilley A. 1997. Effect of chemical modification of sodium caseinate on diffusivity of aroma compounds in aqueous solutions. J Agric Food Chem 45:2649-53.
    • (1997) J Agric Food Chem , vol.45 , pp. 2649-2653
    • Landy, P.1    Fares, K.2    Lorient, D.3    Voilley, A.4
  • 76
    • 0002422781 scopus 로고
    • Protein-aroma interactions
    • Dickinson E, Lorient D, editors. Cambridge, U.K.: Royal Society of Chemistry
    • Langourieux S, Crouzet J. 1995. Protein-aroma interactions. In: Dickinson E, Lorient D, editors. Food macromolecules and colloids. Cambridge, U.K.: Royal Society of Chemistry, p 123-33.
    • (1995) Food Macromolecules and Colloids , pp. 123-133
    • Langourieux, S.1    Crouzet, J.2
  • 77
    • 0026799535 scopus 로고
    • Interactions between volatile and nonvolatile compounds in the presence of water
    • LeThanh M, Thibeaudeau P, Thibaut MA, Voilley A. 1992. Interactions between volatile and nonvolatile compounds in the presence of water. Food Chem 43:129-35.
    • (1992) Food Chem , vol.43 , pp. 129-135
    • Lethanh, M.1    Thibeaudeau, P.2    Thibaut, M.A.3    Voilley, A.4
  • 79
    • 0033758396 scopus 로고    scopus 로고
    • Interaction of vanillin with soy and dairy proteins in aqueous model systems: A thermodynamic study
    • Li Z, Grün IU, Fernando LN. 2000. Interaction of vanillin with soy and dairy proteins in aqueous model systems: a thermodynamic study. J Food Sci 65:997-1001.
    • (2000) J Food Sci , vol.65 , pp. 997-1001
    • Li, Z.1    Grün, I.U.2    Fernando, L.N.3
  • 80
    • 10044271359 scopus 로고    scopus 로고
    • On-line monitoring of volatile organic compounds at pptv levels by means of proton-transfer-reaction mass spectrometry (PTR-MS)-medical applications, food control and environmental research
    • Lindinger W, Hansel A, Jordan A. 1998. On-line monitoring of volatile organic compounds at pptv levels by means of proton-transfer-reaction mass spectrometry (PTR-MS)-medical applications, food control and environmental research. Int J Mass Spectrom 173:191-241.
    • (1998) Int J Mass Spectrom , vol.173 , pp. 191-241
    • Lindinger, W.1    Hansel, A.2    Jordan, A.3
  • 81
    • 0027321287 scopus 로고
    • Measurement of volatile release in the mouth
    • Linforth RST, Taylor AJ. 1993. Measurement of volatile release in the mouth. Food Chem 48:115-20.
    • (1993) Food Chem , vol.48 , pp. 115-120
    • Linforth, R.S.T.1    Taylor, A.J.2
  • 82
    • 29544443468 scopus 로고    scopus 로고
    • High hydrostatic pressure affects flavor-binding properties of whey protein concentrate
    • Liu X, Powers JR, Swanson BG, Hill HH, Clark S. 2005a. High hydrostatic pressure affects flavor-binding properties of whey protein concentrate. J Food Sci 70:C581-5.
    • (2005) J Food Sci , vol.70
    • Liu, X.1    Powers, J.R.2    Swanson, B.G.3    Hill, H.H.4    Clark, S.5
  • 84
    • 0041032340 scopus 로고    scopus 로고
    • Infrared spectroscopic study of β-lactoglobulin interactions with flavor compounds
    • Roberts DD, Taylor AJ, editors. Washington, D.C.: American Chemical Society
    • Lübke M, Guichard E, Le Quéré JL. 2000. Infrared spectroscopic study of β-lactoglobulin interactions with flavor compounds. In: Roberts DD, Taylor AJ, editors. Flavor release. Washington, D.C.: American Chemical Society. p 282-92.
    • (2000) Flavor Release , pp. 282-292
    • Lübke, M.1    Guichard, E.2    Le Quéré, J.L.3
  • 85
    • 0037145918 scopus 로고    scopus 로고
    • Nuclear magnetic resonance spectroscopic study of β-lactoglobulin interactions with two flavor compounds, γ-decalactone and β-ionone
    • Lübke M, Guichard E, Tromelin A, Le Quéré JL. 2002. Nuclear magnetic resonance spectroscopic study of β-lactoglobulin interactions with two flavor compounds, γ-decalactone and β-ionone. J Agric Food Chem 50:7094-9.
    • (2002) J Agric Food Chem , vol.50 , pp. 7094-7099
    • Lübke, M.1    Guichard, E.2    Tromelin, A.3    Le Quéré, J.L.4
  • 86
    • 0014902153 scopus 로고
    • Volatile flavoring substances in foodstuffs
    • Maier HG. 1970. Volatile flavoring substances in foodstuffs. Angew Chem Int Ed Engl 9:917-26.
    • (1970) Angew Chem Int Ed Engl , vol.9 , pp. 917-926
    • Maier, H.G.1
  • 87
    • 0001929236 scopus 로고
    • Bindung flüchtiger Aromastoffe an Lebensmittel
    • Maier HG. 1972. Bindung flüchtiger Aromastoffe an Lebensmittel. Lebensm-Wiss Technol 5:1-6.
    • (1972) Lebensm-Wiss Technol , vol.5 , pp. 1-6
    • Maier, H.G.1
  • 88
    • 0011428117 scopus 로고
    • Sorption of volatile aroma constituents by foods. 7. Aliphatic aldehydes
    • Maier HG. 1973. Sorption of volatile aroma constituents by foods. 7. Aliphatic aldehydes. Z Lebensm-Unters Forsch 151:384-6.
    • (1973) Z Lebensm-Unters Forsch , vol.151 , pp. 384-386
    • Maier, H.G.1
  • 89
    • 0002084154 scopus 로고
    • Binding of volatile aroma substances to nutrients and foodstuffs
    • Maarse H, Groenen PJ, editors. Wageningen: Pudoc
    • Maier HG. 1975. Binding of volatile aroma substances to nutrients and foodstuffs. In: Maarse H, Groenen PJ, editors. Aroma research. Wageningen: Pudoc. p 143-57.
    • (1975) Aroma Research , pp. 143-157
    • Maier, H.G.1
  • 90
  • 91
    • 0000773537 scopus 로고
    • Vanillin interaction with milk protein isolates in sweetened drinks
    • McNeill VL, Schmidt KA. 1993. Vanillin interaction with milk protein isolates in sweetened drinks. J Food Sci 58:1142-4, 1147.
    • (1993) J Food Sci , vol.58 , pp. 1142-1144
    • McNeill, V.L.1    Schmidt, K.A.2
  • 92
    • 12344326101 scopus 로고    scopus 로고
    • Aroma release and retronasal perception during and after consumption of flavored whey protein gels with different textures. 1. In vivo release analysis
    • Mestres M, Moran N, Jordan A, Buettner A. 2005. Aroma release and retronasal perception during and after consumption of flavored whey protein gels with different textures. 1. In vivo release analysis. J Agric Food Chem 53:403-9.
    • (2005) J Agric Food Chem , vol.53 , pp. 403-409
    • Mestres, M.1    Moran, N.2    Jordan, A.3    Buettner, A.4
  • 93
    • 0037984772 scopus 로고    scopus 로고
    • Partition of five aroma compounds between air and skim milk, anhydrous milk fat or full-fat cream
    • Meynier A, Garillon A, Lethuaut L, Genot C. 2003. Partition of five aroma compounds between air and skim milk, anhydrous milk fat or full-fat cream. Lait 83:223-35.
    • (2003) Lait , vol.83 , pp. 223-235
    • Meynier, A.1    Garillon, A.2    Lethuaut, L.3    Genot, C.4
  • 94
    • 2542471901 scopus 로고    scopus 로고
    • Hexanal and t-2-hexenal form covalent bonds with whey proteins and sodium caseinate in aqueous solution
    • Meynier A, Rampon V, Dalgalarrondo M, Genot C. 2004. Hexanal and t-2-hexenal form covalent bonds with whey proteins and sodium caseinate in aqueous solution. Int Dairy J 14:681-90.
    • (2004) Int Dairy J , vol.14 , pp. 681-690
    • Meynier, A.1    Rampon, V.2    Dalgalarrondo, M.3    Genot, C.4
  • 95
    • 0000240706 scopus 로고
    • Interaction of selected flavor compounds with whey proteins
    • Mills OE, Solms J. 1984. Interaction of selected flavor compounds with whey proteins. Lebensm-Wiss Technol 17:331-5.
    • (1984) Lebensm-Wiss Technol , vol.17 , pp. 331-335
    • Mills, O.E.1    Solms, J.2
  • 96
    • 0037462049 scopus 로고    scopus 로고
    • Effects of hydration, lipids, and temperature on the binding of the volatile aroma terpenes by β-lactoglobulin powders
    • Mitonov NA, Breus W, Gorbatchuk W, Solomonov BN, Haertle T. 2003. Effects of hydration, lipids, and temperature on the binding of the volatile aroma terpenes by β-lactoglobulin powders. J Agric Food Chem 51:2665-73.
    • (2003) J Agric Food Chem , vol.51 , pp. 2665-2673
    • Mitonov, N.A.1    Breus, W.2    Gorbatchuk, W.3    Solomonov, B.N.4    Haertle, T.5
  • 97
    • 0014672123 scopus 로고
    • Hydrophobic binding of hydrocarbons by proteins I. Relationship of hydrocarbon structure
    • Mohammadzadeh-K A, Feeney RE, Smith LM. 1969a. Hydrophobic binding of hydrocarbons by proteins I. Relationship of hydrocarbon structure. Biochim Biophys Acta 194:246-55.
    • (1969) Biochim Biophys Acta , vol.194 , pp. 246-255
    • Mohammadzadeh-K, A.1    Feeney, R.E.2    Smith, L.M.3
  • 98
    • 0014672035 scopus 로고
    • Hydrophobic binding of hydrocarbons by proteins II. Relationship of protein structure
    • Mohammadzadeh-K A, Smith LM, Feeney RE. 1969b. Hydrophobic binding of hydrocarbons by proteins II. Relationship of protein structure. Biochim Biophys Acta 194:256-64.
    • (1969) Biochim Biophys Acta , vol.194 , pp. 256-264
    • Mohammadzadeh-K, A.1    Smith, L.M.2    Feeney, R.E.3
  • 100
    • 0023661017 scopus 로고
    • Crystal-structure of the trigonal form of bovine β-lactoglobulin and of its complex with retinol at 2.5 Å resolution
    • Monaco HL, Zanotti G, Spadon P, Bolognesi M, Sawyer L, Eliopoulos EE. 1987. Crystal-structure of the trigonal form of bovine β-lactoglobulin and of its complex with retinol at 2.5 Å resolution. J Mol Biol 197:695-706.
    • (1987) J Mol Biol , vol.197 , pp. 695-706
    • Monaco, H.L.1    Zanotti, G.2    Spadon, P.3    Bolognesi, M.4    Sawyer, L.5    Eliopoulos, E.E.6
  • 101
    • 0016794967 scopus 로고
    • Bovine serum albumin: Study of the fatty acid and steroid binding sites using spin-labelled lipids
    • Morrisett JD, Pownall HJ, Gotto AMG. 1975. Bovine serum albumin: study of the fatty acid and steroid binding sites using spin-labelled lipids. J Biol Chem 250:2487-94.
    • (1975) J Biol Chem , vol.250 , pp. 2487-2494
    • Morrisett, J.D.1    Pownall, H.J.2    Gotto, A.M.G.3
  • 102
    • 0001677399 scopus 로고    scopus 로고
    • Interaction of thiol and disulfide flavor compounds with food components
    • Mottram DS, Szauman-Szumski C, Dodson A. 1996. Interaction of thiol and disulfide flavor compounds with food components. J Agric Food Chem 44:2349-51.
    • (1996) J Agric Food Chem , vol.44 , pp. 2349-2351
    • Mottram, D.S.1    Szauman-Szumski, C.2    Dodson, A.3
  • 103
    • 0001006160 scopus 로고
    • Production, functional properties and utilization of milk protein products
    • Fox PF, editor. New York: Elsevier Applied Science
    • Mulvihill DM. 1992. Production, functional properties and utilization of milk protein products. In: Fox PF, editor. Advanced dairy chemistry-1: Proteins. New York: Elsevier Applied Science, p 369-404.
    • (1992) Advanced Dairy Chemistry-1: Proteins , pp. 369-404
    • Mulvihill, D.M.1
  • 104
    • 0034849396 scopus 로고    scopus 로고
    • Interaction of β-lactoglobulin with small hydrophobic ligands as monitored by fluorometry and equilibrium dialysis: Nonlinear quenching effects related to protein-protein association
    • Muresan S, van der Bent A, de Wolf FA. 2001. Interaction of β-lactoglobulin with small hydrophobic ligands as monitored by fluorometry and equilibrium dialysis: nonlinear quenching effects related to protein-protein association. J Agric Food Chem 49:2609-18.
    • (2001) J Agric Food Chem , vol.49 , pp. 2609-2618
    • Muresan, S.1    Van Der Bent, A.2    De Wolf, F.A.3
  • 105
    • 0039729623 scopus 로고
    • Some considerations in interpretation of direct headspace gas chromatographic analysis of food volatiles
    • Nawar WW. 1966. Some considerations in interpretation of direct headspace gas chromatographic analysis of food volatiles. Food Technol 20:115-7.
    • (1966) Food Technol , vol.20 , pp. 115-117
    • Nawar, W.W.1
  • 106
    • 84985287348 scopus 로고
    • Binding of vanillin by fababean proteins
    • Ng PKW, Hoehn E, Bushuk W. 1989a. Binding of vanillin by fababean proteins. J Food Sci 54:105-7.
    • (1989) J Food Sci , vol.54 , pp. 105-107
    • Ng, P.K.W.1    Hoehn, E.2    Bushuk, W.3
  • 107
    • 84985251676 scopus 로고
    • Sensory evaluation of binding of vanillin by fababean proteins
    • Ng PKW, Hoehn E, Bushuk W. 1989b. Sensory evaluation of binding of vanillin by fababean proteins. J Food Sci 54:324-5, 346.
    • (1989) J Food Sci , vol.54 , pp. 324-325
    • Ng, P.K.W.1    Hoehn, E.2    Bushuk, W.3
  • 108
    • 0024613601 scopus 로고
    • 3-Dimensional arrangement of conserved amino acid residues in a superfamily of specific ligand-binding proteins
    • North ACT. 1989. 3-Dimensional arrangement of conserved amino acid residues in a superfamily of specific ligand-binding proteins. Int J Biol Macromol 11:56-8.
    • (1989) Int J Biol Macromol , vol.11 , pp. 56-58
    • North, A.C.T.1
  • 109
    • 84985258627 scopus 로고
    • Temperature effect on binding of volatile flavor compounds to soy protein in aqueous model systems
    • O'Keefe SF, Resurreccion AP, Wilson LA, Murphy PA. 1991a. Temperature effect on binding of volatile flavor compounds to soy protein in aqueous model systems. J Food Sci 56:802-6.
    • (1991) J Food Sci , vol.56 , pp. 802-806
    • O'Keefe, S.F.1    Resurreccion, A.P.2    Wilson, L.A.3    Murphy, P.A.4
  • 110
    • 0000121624 scopus 로고
    • Determination of the binding of hexanal to soy glycinin and β-conglycinin in an aqueous model system using a headspace technique
    • O'Keefe SF, Wilson LA, Resurreccion AP, Murphy PA. 1991b. Determination of the binding of hexanal to soy glycinin and β-conglycinin in an aqueous model system using a headspace technique. J Agric Food Chem 39:1022-8.
    • (1991) J Agric Food Chem , vol.39 , pp. 1022-1028
    • O'Keefe, S.F.1    Wilson, L.A.2    Resurreccion, A.P.3    Murphy, P.A.4
  • 111
    • 33845282222 scopus 로고
    • Binding of alkanone flavors to β-lactoglobulin-effects of conformational and chemical modification
    • O'Neill TE, Kinsella JE. 1987. Binding of alkanone flavors to β-lactoglobulin-effects of conformational and chemical modification. J Agric Food Chem 35:770-4.
    • (1987) J Agric Food Chem , vol.35 , pp. 770-774
    • O'Neill, T.E.1    Kinsella, J.E.2
  • 112
    • 84987306776 scopus 로고
    • Effect of heat treatment and modification on conformation and flavor binding by β-lactoglobulin
    • O'Neill TE, Kinsella JE. 1988. Effect of heat treatment and modification on conformation and flavor binding by β-lactoglobulin. J Food Sci 53:906-9.
    • (1988) J Food Sci , vol.53 , pp. 906-909
    • O'Neill, T.E.1    Kinsella, J.E.2
  • 115
    • 0000080621 scopus 로고    scopus 로고
    • Measurement of interactions between β-lactoglobulin and flavor compounds (esters, acids, and pyrazines) by affinity and exclusion size chromatography
    • Pelletier E, Sostmann K, Guichard E. 1998. Measurement of interactions between β-lactoglobulin and flavor compounds (esters, acids, and pyrazines) by affinity and exclusion size chromatography. J Agric Food Chem 46:1506-9.
    • (1998) J Agric Food Chem , vol.46 , pp. 1506-1509
    • Pelletier, E.1    Sostmann, K.2    Guichard, E.3
  • 118
    • 0027599484 scopus 로고
    • The role of ingredient-flavor interactions in the development of fat-free foods
    • Plug H, Haring P. 1993. The role of ingredient-flavor interactions in the development of fat-free foods. Trends Food Sci Technol 4:150-2.
    • (1993) Trends Food Sci Technol , vol.4 , pp. 150-152
    • Plug, H.1    Haring, P.2
  • 119
    • 0017073254 scopus 로고
    • Changes of sensory value by interaction of alkanals with amino acids and proteins
    • Pokorný J, Luan NT, Kondratenko SS, Janicek G. 1976. Changes of sensory value by interaction of alkanals with amino acids and proteins. Nahrung 20:267-72.
    • (1976) Nahrung , vol.20 , pp. 267-272
    • Pokorný, J.1    Luan, N.T.2    Kondratenko, S.S.3    Janicek, G.4
  • 120
    • 0037164025 scopus 로고    scopus 로고
    • Computerized apparatus for measuring dynamic flavor release from liquid food matrices
    • Rabe S, Krings U, Banavara DS, Berger RG. 2002. Computerized apparatus for measuring dynamic flavor release from liquid food matrices. J Agric Food Chem 50:6440-7.
    • (2002) J Agric Food Chem , vol.50 , pp. 6440-6447
    • Rabe, S.1    Krings, U.2    Banavara, D.S.3    Berger, R.G.4
  • 122
    • 85010250962 scopus 로고
    • Flavor retention during drying
    • Reineccius GA, Coulter ST. 1969. Flavor retention during drying. J Dairy Sci 52:1219-23.
    • (1969) J Dairy Sci , vol.52 , pp. 1219-1223
    • Reineccius, G.A.1    Coulter, S.T.2
  • 123
    • 0034423877 scopus 로고    scopus 로고
    • Interactions between β-lactoglobulin and flavour compounds of different chemical classes. Impact of the protein on the odour perception of vanillin and eugenol
    • Reiners J, Nicklaus S, Guichard E. 2000. Interactions between β-lactoglobulin and flavour compounds of different chemical classes. Impact of the protein on the odour perception of vanillin and eugenol. Lait 80:347-60.
    • (2000) Lait , vol.80 , pp. 347-360
    • Reiners, J.1    Nicklaus, S.2    Guichard, E.3
  • 124
    • 0001524414 scopus 로고
    • Simulation of retronasal aroma using a modified headspace technique-investigating the effects of saliva, temperature, shearing, and oil on flavor release
    • Roberts DD, Acree TE. 1995. Simulation of retronasal aroma using a modified headspace technique-investigating the effects of saliva, temperature, shearing, and oil on flavor release. J Agric Food Chem 43:2179-86.
    • (1995) J Agric Food Chem , vol.43 , pp. 2179-2186
    • Roberts, D.D.1    Acree, T.E.2
  • 125
    • 0041032334 scopus 로고    scopus 로고
    • Relative influence of milk components on flavor compound volatility
    • Roberts DD, Taylor AJ, editors. Washington, D.C.: American Chemical Society
    • Roberts DD, Pollien P. 2000. Relative influence of milk components on flavor compound volatility. In: Roberts DD, Taylor AJ, editors. Flavor release. Washington, D.C.: American Chemical Society, p 321-32.
    • (2000) Flavor Release , pp. 321-332
    • Roberts, D.D.1    Pollien, P.2
  • 126
    • 0033919327 scopus 로고    scopus 로고
    • Solid-phase microextraction method development for headspace analysis of volatile flavor compounds
    • Roberts DD, Pollien P, Milo C. 2000. Solid-phase microextraction method development for headspace analysis of volatile flavor compounds. J Agric Food Chem 48:2430-7.
    • (2000) J Agric Food Chem , vol.48 , pp. 2430-2437
    • Roberts, D.D.1    Pollien, P.2    Milo, C.3
  • 127
    • 0015501847 scopus 로고
    • Aromatic hydrophobes and β-lactoglobulin A-thermodynamics of binding
    • Robillard KA, Wishnia A. 1972. Aromatic hydrophobes and β-lactoglobulin A-thermodynamics of binding. Biochemistry 11:3835-40.
    • (1972) Biochemistry , vol.11 , pp. 3835-3840
    • Robillard, K.A.1    Wishnia, A.2
  • 129
    • 84969001783 scopus 로고
    • The attractions of proteins for small molecules and ions
    • Scatchard G. 1949. The attractions of proteins for small molecules and ions. Ann N Y Acad Sci 51:660-72.
    • (1949) Ann N Y Acad Sci , vol.51 , pp. 660-672
    • Scatchard, G.1
  • 130
    • 0036838129 scopus 로고    scopus 로고
    • Binding of aroma compounds with legumin. 1. Binding of hexyl acetate with 11S globulin depending on the protein molecular state in aqueous medium
    • Semenova MG, Antipova AS, Misharina TA, Golovnya RV. 2002a. Binding of aroma compounds with legumin. 1. Binding of hexyl acetate with 11S globulin depending on the protein molecular state in aqueous medium. Food Hydrocolloids 16:557-64.
    • (2002) Food Hydrocolloids , vol.16 , pp. 557-564
    • Semenova, M.G.1    Antipova, A.S.2    Misharina, T.A.3    Golovnya, R.V.4
  • 131
    • 0036837951 scopus 로고    scopus 로고
    • Binding of aroma com pounds with legumin. II. Effect of hexyl acetate on thermodynamic properties of US globulin in aqueous medium
    • Semenova MG, Antipova AS, Wasserman LA, Misharina TA, Golovnya RV. 2002b. Binding of aroma com pounds with legumin. II. Effect of hexyl acetate on thermodynamic properties of US globulin in aqueous medium. Food Hydrocolloids 16:565-71.
    • (2002) Food Hydrocolloids , vol.16 , pp. 565-571
    • Semenova, M.G.1    Antipova, A.S.2    Wasserman, L.A.3    Misharina, T.A.4    Golovnya, R.V.5
  • 133
    • 0041186294 scopus 로고
    • Improving the flavour acceptability of reduced-fat foods
    • Shamil S, Kilcast D. 1992. Improving the flavour acceptability of reduced-fat foods. Nutr Food Sci 4:7-10.
    • (1992) Nutr Food Sci , vol.4 , pp. 7-10
    • Shamil, S.1    Kilcast, D.2
  • 135
    • 0022908691 scopus 로고
    • Activity coefficients of aroma compounds in model food systems
    • Sorrentino F, Voilley A, Richon D. 1986. Activity coefficients of aroma compounds in model food systems. AIChE J 32:1988-93.
    • (1986) AIChE J , vol.32 , pp. 1988-1993
    • Sorrentino, F.1    Voilley, A.2    Richon, D.3
  • 136
    • 0032143329 scopus 로고    scopus 로고
    • Immobilized β-lactoglobulin on a HPLC-column: A rapid way to determine protein-flavour interactions
    • Sostmann K, Guichard E. 1998. Immobilized β-lactoglobulin on a HPLC-column: a rapid way to determine protein-flavour interactions. Food Chem 62:509-13.
    • (1998) Food Chem , vol.62 , pp. 509-513
    • Sostmann, K.1    Guichard, E.2
  • 137
    • 0016691920 scopus 로고
    • Fatty acid binding to plasma albumin
    • Spector AA. 1975. Fatty acid binding to plasma albumin. J Lipid Res 16:165-79.
    • (1975) J Lipid Res , vol.16 , pp. 165-179
    • Spector, A.A.1
  • 138
    • 0014770081 scopus 로고
    • Binding of long chain fatty acids to β-lactoglobulin
    • Spector AA, Fletcher JE. 1970. Binding of long chain fatty acids to β-lactoglobulin. Lipids 5:403-11.
    • (1970) Lipids , vol.5 , pp. 403-411
    • Spector, A.A.1    Fletcher, J.E.2
  • 139
    • 0014440335 scopus 로고
    • Binding of long-chain fatty acids to bovine serum albumin
    • Spector AA, John K, Fletcher JE. 1969. Binding of long-chain fatty acids to bovine serum albumin. J Lipid Res 10:56-67.
    • (1969) J Lipid Res , vol.10 , pp. 56-67
    • Spector, A.A.1    John, K.2    Fletcher, J.E.3
  • 141
    • 0030118497 scopus 로고    scopus 로고
    • Modern analyses and binding studies of flavour volatiles with particular reference to dairy protein products
    • Stevenson RJ, Chen XD, Mills OE. 1996. Modern analyses and binding studies of flavour volatiles with particular reference to dairy protein products. Food Res Int 29:265-90.
    • (1996) Food Res Int , vol.29 , pp. 265-290
    • Stevenson, R.J.1    Chen, X.D.2    Mills, O.E.3
  • 142
    • 0002772383 scopus 로고
    • Chemistry of the caseins
    • Fox PF, editor. New York: Elsevier Applied Science
    • Swaisgood HE. 1992. Chemistry of the caseins. In: Fox PF, editor. Advanced dairy chemistry-1: Proteins. New York: Elsevier Applied Science, p 63-110.
    • (1992) Advanced Dairy Chemistry-1: Proteins , pp. 63-110
    • Swaisgood, H.E.1
  • 143
    • 0039253808 scopus 로고    scopus 로고
    • Techniques for measuring volatile release in vivo during consumption of food
    • Roberts DD, Taylor AJ, editors. Washington: American Chemical Society
    • Taylor AJ, Linforth RST. 2000. Techniques for measuring volatile release in vivo during consumption of food. In: Roberts DD, Taylor AJ, editors. Flavor release. Washington: American Chemical Society, p 8-21.
    • (2000) Flavor Release , pp. 8-21
    • Taylor, A.J.1    Linforth, R.S.T.2
  • 144
    • 0034670213 scopus 로고    scopus 로고
    • Atmospheric pressure chemical ionisation mass spectrometry for in vivo analysis of volatile flavour release
    • Taylor AJ, Linforth RST, Harvey BA, Blake B. 2000. Atmospheric pressure chemical ionisation mass spectrometry for in vivo analysis of volatile flavour release. Food Chem 71:327-38.
    • (2000) Food Chem , vol.71 , pp. 327-338
    • Taylor, A.J.1    Linforth, R.S.T.2    Harvey, B.A.3    Blake, B.4
  • 145
    • 0345794019 scopus 로고    scopus 로고
    • Applications of high-hydrostatic pressure on milkand dairy products
    • Trujillo AJ. 2002. Applications of high-hydrostatic pressure on milkand dairy products. High Press Res 22:619-26.
    • (2002) High Press Res , vol.22 , pp. 619-626
    • Trujillo, A.J.1
  • 146
    • 0036838159 scopus 로고    scopus 로고
    • Influence of β-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
    • van Ruth SM, Villeneuve E. 2002. Influence of β-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 79:157-64.
    • (2002) Food Chem , vol.79 , pp. 157-164
    • Van Ruth, S.M.1    Villeneuve, E.2
  • 147
    • 0036306701 scopus 로고    scopus 로고
    • Influence of composition and structure of oil-in-water emulsions on retention of aroma compounds
    • van Ruth SM, de Vries G, Geary M, Giannouli P. 2002. Influence of composition and structure of oil-in-water emulsions on retention of aroma compounds. J Sci Food Agric 82:1028-35.
    • (2002) J Sci Food Agric , vol.82 , pp. 1028-1035
    • Van Ruth, S.M.1    De Vries, G.2    Geary, M.3    Giannouli, P.4
  • 148
    • 0000319575 scopus 로고
    • Interactions between aroma substances and macromolecules in a model wine
    • Voilley A, Beghin V, Charpentier C, Peyron D. 1991. Interactions between aroma substances and macromolecules in a model wine. Lebensm-Wiss Technol 24:469-72.
    • (1991) Lebensm-Wiss Technol , vol.24 , pp. 469-472
    • Voilley, A.1    Beghin, V.2    Charpentier, C.3    Peyron, D.4
  • 151
    • 0003040836 scopus 로고    scopus 로고
    • Measurement of the influence of food ingredients on flavour release by headspace gas chromatography-olfactometry
    • Taylor AJ, Mottram DS, editors. Cambridge, U.K.: Royal Society of Chemistry
    • Widder S, Fischer N. 1996. Measurement of the influence of food ingredients on flavour release by headspace gas chromatography-olfactometry. In: Taylor AJ, Mottram DS, editors. Flavour science: recent developments. Cambridge, U.K.: Royal Society of Chemistry, p 405-12.
    • (1996) Flavour Science: Recent Developments , pp. 405-412
    • Widder, S.1    Fischer, N.2
  • 152
    • 0031495841 scopus 로고    scopus 로고
    • Influence of food matrix structure and oral breakdown during mastication on temporal perception of flavor
    • Wilson CE, Brown WE. 1997. Influence of food matrix structure and oral breakdown during mastication on temporal perception of flavor. J Sens Stud 21:69-86.
    • (1997) J Sens Stud , vol.21 , pp. 69-86
    • Wilson, C.E.1    Brown, W.E.2
  • 153
    • 0001493958 scopus 로고
    • Hydrophobic interactions in proteins: Conformation changes in bovine serum albumin below pH 5
    • Wishnia A, Pinder TW. 1964. Hydrophobic interactions in proteins: conformation changes in bovine serum albumin below pH 5. Biochemistry 3:1377-84.
    • (1964) Biochemistry , vol.3 , pp. 1377-1384
    • Wishnia, A.1    Pinder, T.W.2
  • 154
    • 0013905712 scopus 로고
    • Hydrophobic interactions in proteins. The alkane binding site of β-lactoglobulin a and B
    • Wishnia A, Pinder TW. 1966. Hydrophobic interactions in proteins. The alkane binding site of β-lactoglobulin A and B. Biochemistry 5:1534-42.
    • (1966) Biochemistry , vol.5 , pp. 1534-1542
    • Wishnia, A.1    Pinder, T.W.2
  • 155
    • 0004284655 scopus 로고
    • Wong NP, editor. New York: Van Nostrand Reinhold Co.
    • Wong NP, editor. 1988. Fundamentals of dairy chemistry. New York: Van Nostrand Reinhold Co.
    • (1988) Fundamentals of Dairy Chemistry
  • 156
    • 0345313659 scopus 로고    scopus 로고
    • β-lactoglobulin binds palmitate within its central cavity
    • Wu SY, Perez MD, Puyol P, Sawyer L. 1999. β-Lactoglobulin binds palmitate within its central cavity. J Biol Chem 274:170-4.
    • (1999) J Biol Chem , vol.274 , pp. 170-174
    • Wu, S.Y.1    Perez, M.D.2    Puyol, P.3    Sawyer, L.4
  • 157
    • 0141563760 scopus 로고    scopus 로고
    • Ligand and flavor binding functional properties of β-lactoglobulin in the molten globule state induced by high pressure
    • Yang J, Powers JR, Clark S, Dunker AK, Swanson BG. 2003. Ligand and flavor binding functional properties of β-lactoglobulin in the molten globule state induced by high pressure. J Food Sci 68:444-52.
    • (2003) J Food Sci , vol.68 , pp. 444-452
    • Yang, J.1    Powers, J.R.2    Clark, S.3    Dunker, A.K.4    Swanson, B.G.5
  • 158
    • 33751158820 scopus 로고
    • Solid-phase microextraction for flavor analysis
    • Yang XG, Peppard T. 1994. Solid-phase microextraction for flavor analysis. J Agric Food Chem 42:1925-30.
    • (1994) J Agric Food Chem , vol.42 , pp. 1925-1930
    • Yang, X.G.1    Peppard, T.2
  • 159
    • 0000324256 scopus 로고    scopus 로고
    • Assessment of interactions between hydrocolloids and flavor compounds by sensory, headspace, and binding methodologics
    • Yven C, Guichard E, Giboreau A, Roberts DD. 1998. Assessment of interactions between hydrocolloids and flavor compounds by sensory, headspace, and binding methodologics. J Agric Food Chem 46:1510-4.
    • (1998) J Agric Food Chem , vol.46 , pp. 1510-1514
    • Yven, C.1    Guichard, E.2    Giboreau, A.3    Roberts, D.D.4
  • 160
    • 10944254274 scopus 로고
    • Headspace solid-phase microextraction
    • Zhang ZY, Pawliszyn J. 1993. Headspace solid-phase microextraction. Anal Chem 65:1843-52.
    • (1993) Anal Chem , vol.65 , pp. 1843-1852
    • Zhang, Z.Y.1    Pawliszyn, J.2
  • 162
    • 0036186180 scopus 로고    scopus 로고
    • Binding properties of 2-pentyl pyridine to soy protein as measured by solid phase microextraction
    • Zhou A, Boatright WL, Johnson LA, Reuber M. 2002. Binding properties of 2-pentyl pyridine to soy protein as measured by solid phase microextraction. J Food Sci 67:142-5.
    • (2002) J Food Sci , vol.67 , pp. 142-145
    • Zhou, A.1    Boatright, W.L.2    Johnson, L.A.3    Reuber, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.