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Volumn 53, Issue 17, 2005, Pages 6784-6790

NMR relaxation and water self-diffusion studies in whey protein solutions and gels

Author keywords

Diffusion; Gel; NMR; Transverse relaxation; Whey

Indexed keywords

MILK PROTEIN; WATER; WHEY PROTEIN;

EID: 24344440549     PISSN: 00218561     EISSN: None     Source Type: Journal    
DOI: 10.1021/jf050162k     Document Type: Article
Times cited : (46)

References (47)
  • 2
    • 0036704306 scopus 로고    scopus 로고
    • Recent advances in the characterisation of heat-induced aggregates and intermediates of whey proteins
    • De la Fuente, M. A.; Singh, H.; Hemar, Y. Recent advances in the characterisation of heat-induced aggregates and intermediates of whey proteins. Trends Food Sci. Technol. 2002, 13, 262-274.
    • (2002) Trends Food Sci. Technol. , vol.13 , pp. 262-274
    • De La Fuente, M.A.1    Singh, H.2    Hemar, Y.3
  • 3
    • 0024822645 scopus 로고
    • Proteins in whey: Chemical, physical, and functional properties
    • Academic Press: London
    • Kinsella, J. E.; Whitehead, D. M. Proteins in whey: Chemical, physical, and functional properties. In Advances in Food and Nutrition Research; Academic Press: London, 1989.
    • (1989) Advances in Food and Nutrition Research
    • Kinsella, J.E.1    Whitehead, D.M.2
  • 4
    • 85025567869 scopus 로고
    • Fine-stranded and particulate gels of beta-lactoglobulin and whey-protein at varying pH
    • Langton, M.; Hermansson, A. M. Fine-stranded and particulate gels of beta-lactoglobulin and whey-protein at varying pH. Food Hydrocolloids 1992, 5, 523-539.
    • (1992) Food Hydrocolloids , vol.5 , pp. 523-539
    • Langton, M.1    Hermansson, A.M.2
  • 5
    • 0000289106 scopus 로고    scopus 로고
    • Structure of particulate whey protein gels: Effect of NaCl concentration, pH, heating temperature, and protein composition
    • Verheul, M.; Roefs, S. Structure of particulate whey protein gels: Effect of NaCl concentration, pH, heating temperature, and protein composition. J. Agric. Food Chem. 1998, 46, 4909-4916.
    • (1998) J. Agric. Food Chem. , vol.46 , pp. 4909-4916
    • Verheul, M.1    Roefs, S.2
  • 6
    • 85024659041 scopus 로고
    • Factors that determine the fracture properties and microstructure of globular protein gels
    • Foegeding, E. A.; Rowland, E. L.; Hardin, C. C. Factors that determine the fracture properties and microstructure of globular protein gels. Food Hydrocolloids 1995, 9, 237-249.
    • (1995) Food Hydrocolloids , vol.9 , pp. 237-249
    • Foegeding, E.A.1    Rowland, E.L.2    Hardin, C.C.3
  • 8
    • 0342467949 scopus 로고    scopus 로고
    • Heat-induced gelation of whey protein isolates (WPI): Effect of NaCl and protein concentration
    • Puyol, P.; Perez, M. D.; Horne, D. S. Heat-induced gelation of whey protein isolates (WPI): Effect of NaCl and protein concentration. Food Hydrocolloids 2001, 15, 233-237.
    • (2001) Food Hydrocolloids , vol.15 , pp. 233-237
    • Puyol, P.1    Perez, M.D.2    Horne, D.S.3
  • 9
    • 0036328703 scopus 로고    scopus 로고
    • Influence of NaCl on optical properties, large-strain rheology and water holding capacity of heat-induced whey protein isolate gels
    • Chantrapornchai, W.; McClements, D. J. Influence of NaCl on optical properties, large-strain rheology and water holding capacity of heat-induced whey protein isolate gels. Food Hydrocolloids 2002, 16, 467-476.
    • (2002) Food Hydrocolloids , vol.16 , pp. 467-476
    • Chantrapornchai, W.1    McClements, D.J.2
  • 10
    • 0007674510 scopus 로고    scopus 로고
    • Structure of whey protein gels, studied by permeability, scanning electron microscopy and rheology
    • Verheul, M.; Roefs, S. Structure of whey protein gels, studied by permeability, scanning electron microscopy and rheology. Food hydrocolloids 1998, 12, 17-24.
    • (1998) Food Hydrocolloids , vol.12 , pp. 17-24
    • Verheul, M.1    Roefs, S.2
  • 11
    • 0031498272 scopus 로고    scopus 로고
    • Pulsed field gradient nuclear magnetic resonance as a tool for studying translational diffusion: Part 1. Basic theory
    • Price, W. S. Pulsed field gradient nuclear magnetic resonance as a tool for studying translational diffusion: Part 1. Basic theory. Concepts Magn. Reson. 1997, 9, 299-336.
    • (1997) Concepts Magn. Reson. , vol.9 , pp. 299-336
    • Price, W.S.1
  • 12
  • 13
    • 0032100931 scopus 로고    scopus 로고
    • Microstructural characterization of starch systems by NMR relaxation and Q-SPACE microscopy
    • Hills, B. P.; Godward, J.; Manning, C. E.; Biechlin, J. L.; Wright, K. M. Microstructural characterization of starch systems by NMR relaxation and Q-SPACE microscopy. Magn. Reson. Imaging 1998, 16, 557-564.
    • (1998) Magn. Reson. Imaging , vol.16 , pp. 557-564
    • Hills, B.P.1    Godward, J.2    Manning, C.E.3    Biechlin, J.L.4    Wright, K.M.5
  • 14
    • 0036623755 scopus 로고    scopus 로고
    • Changes of cellulose fiber wall structure during drying investigated using NMR self-diffusion and relaxation experiments
    • Topgaard, D.; Soderman, O. Changes of cellulose fiber wall structure during drying investigated using NMR self-diffusion and relaxation experiments. Cellulose 2002, 9, 139-147.
    • (2002) Cellulose , vol.9 , pp. 139-147
    • Topgaard, D.1    Soderman, O.2
  • 16
    • 21344487568 scopus 로고
    • Geometrical restrictions of water diffusion in aqueous protein systems. A study using NMR field-gradient techniques
    • Kimmich, R.; Klammer, F.; Skirda, V. D.; Serebrennikova, I. A.; Maklakov, A. I.; Fatkullin, N. Geometrical restrictions of water diffusion in aqueous protein systems. A study using NMR field-gradient techniques. Appl. Magn. Reson. 1993, 4, 425-440.
    • (1993) Appl. Magn. Reson. , vol.4 , pp. 425-440
    • Kimmich, R.1    Klammer, F.2    Skirda, V.D.3    Serebrennikova, I.A.4    Maklakov, A.I.5    Fatkullin, N.6
  • 17
    • 0000604735 scopus 로고
    • Self-diffusion measurements on bovine serum albumin solutions and gels using a pulsed gradient spin-echo NMR technique
    • Brown, W.; Stilbs, P. Self-diffusion measurements on bovine serum albumin solutions and gels using a pulsed gradient spin-echo NMR technique. Chem. Scr. 1982, 19, 161-163.
    • (1982) Chem. Scr. , vol.19 , pp. 161-163
    • Brown, W.1    Stilbs, P.2
  • 20
    • 0033359921 scopus 로고    scopus 로고
    • Physical models of diffusion for polymer solutions, gels and solids
    • Masaro, L.; Zhu, X. X. Physical models of diffusion for polymer solutions, gels and solids. Prog. Polym. Sci. 1999, 24, 731-775.
    • (1999) Prog. Polym. Sci. , vol.24 , pp. 731-775
    • Masaro, L.1    Zhu, X.X.2
  • 21
    • 0020163001 scopus 로고
    • Diffusion in gels
    • Muhr, A. H.; Blanshard, J. M. V. Diffusion in gels. Polymer 1982, 23, 1012-1026.
    • (1982) Polymer , vol.23 , pp. 1012-1026
    • Muhr, A.H.1    Blanshard, J.M.V.2
  • 24
    • 33847534249 scopus 로고
    • Effects of diffusion on free precession in nuclear magnetic resonance experiments
    • Carr, H. Y.; Purcell, E. M. Effects of diffusion on free precession in nuclear magnetic resonance experiments. Phys. Rev. 1954, 94, 630-638.
    • (1954) Phys. Rev. , vol.94 , pp. 630-638
    • Carr, H.Y.1    Purcell, E.M.2
  • 25
    • 0002899752 scopus 로고
    • Compensation for pulse imperfections in Carr-Purcell NMR experiments
    • Meiboom, S. G. D. Compensation for pulse imperfections in Carr-Purcell NMR experiments. Rev. Sci. Instrum. 1958, 29, 688.
    • (1958) Rev. Sci. Instrum. , vol.29 , pp. 688
    • Meiboom, S.G.D.1
  • 26
    • 36849101148 scopus 로고
    • Use of stimulated echo in NMR diffusion studies
    • Tanner, J. E. Use of stimulated echo in NMR diffusion studies. J. Chem. Phys. 1970, 52 (5), 2523-2526.
    • (1970) J. Chem. Phys. , vol.52 , Issue.5 , pp. 2523-2526
    • Tanner, J.E.1
  • 27
    • 84947139151 scopus 로고
    • The effects of proteins on the proton NMR transverse relaxation times of water. I. Native bovine serum albumine
    • Hills, B. P.; Takacs, S. F.; Belton, P. S. The effects of proteins on the proton NMR transverse relaxation times of water. I. Native bovine serum albumine. Mol. Phys. 1989, 67, 903-918.
    • (1989) Mol. Phys. , vol.67 , pp. 903-918
    • Hills, B.P.1    Takacs, S.F.2    Belton, P.S.3
  • 28
    • 0542416081 scopus 로고
    • The effects of proteins on the proton NMR transverse relaxation time of water. II. Protein aggregation
    • Hills, B. P.; Takacs, S. F.; Belton, P. S. The effects of proteins on the proton NMR transverse relaxation time of water. II. Protein aggregation. Mol. Phys. 1989, 67, 919-937.
    • (1989) Mol. Phys. , vol.67 , pp. 919-937
    • Hills, B.P.1    Takacs, S.F.2    Belton, P.S.3
  • 29
    • 0025310597 scopus 로고
    • A new interpretation of proton NMR relaxation time measurements of water in food
    • Hills, B. P.; Takacs, S. F.; Belton, P. S. A new interpretation of proton NMR relaxation time measurements of water in food. Food Chem. 1990, 37, 95-111.
    • (1990) Food Chem. , vol.37 , pp. 95-111
    • Hills, B.P.1    Takacs, S.F.2    Belton, P.S.3
  • 30
    • 0025414155 scopus 로고
    • Molecular theory for nuclear magnetic relaxation in protein solutions and tissue: Surface diffusion and free-volume analogy
    • Kimmich, R.; Nusser, W.; Gneiting, T. Molecular theory for nuclear magnetic relaxation in protein solutions and tissue: Surface diffusion and free-volume analogy. Colloids Surf. 1990, 45, 283-302.
    • (1990) Colloids Surf. , vol.45 , pp. 283-302
    • Kimmich, R.1    Nusser, W.2    Gneiting, T.3
  • 31
    • 0030919951 scopus 로고    scopus 로고
    • 1H magnetic relaxation dispersion in protein solutions. A quantitative assessment of internal hydration, proton exchange, and cross-relaxation
    • 1H magnetic relaxation dispersion in protein solutions. A quantitative assessment of internal hydration, proton exchange, and cross-relaxation. J. Am. Chem. Soc. 1997, 119, 3122-3134.
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 3122-3134
    • Venu, K.1    Denisov, V.P.2    Halle, B.3
  • 32
    • 0542435321 scopus 로고
    • Magnetic resonance in food science
    • John Wiley & Sons: New York
    • Hills, B. P. Magnetic resonance in food science. In Dynamics of Solutions and Fluid Mixtures by NMR; John Wiley & Sons: New York, 1995; pp 549-580.
    • (1995) Dynamics of Solutions and Fluid Mixtures by NMR , pp. 549-580
    • Hills, B.P.1
  • 33
    • 0027977445 scopus 로고
    • NMR studies of protein hydration
    • Belton, P. S. NMR studies of protein hydration. Prog. Biophys. Mol. Biol. 1994, 61, 61-79.
    • (1994) Prog. Biophys. Mol. Biol. , vol.61 , pp. 61-79
    • Belton, P.S.1
  • 34
    • 84976032113 scopus 로고
    • Multinuclear NMR study of the pH dependent water state in skim milk and caseinate solutions
    • Mariette, F.; Tellier, C.; Brule, G.; Marchal, P. Multinuclear NMR study of the pH dependent water state in skim milk and caseinate solutions. J. Dairy Res. 1993, 60, 175-188.
    • (1993) J. Dairy Res. , vol.60 , pp. 175-188
    • Mariette, F.1    Tellier, C.2    Brule, G.3    Marchal, P.4
  • 35
    • 4143144372 scopus 로고    scopus 로고
    • 1H nuclear magnetic resonance relaxometry study of water state in milk protein mixtures
    • 1H nuclear magnetic resonance relaxometry study of water state in milk protein mixtures. J. Agric. Food Chem. 2004, 52, 5449-5455.
    • (2004) J. Agric. Food Chem. , vol.52 , pp. 5449-5455
    • Le Dean, A.1    Mariette, F.2    Marin, M.3
  • 37
    • 0000371762 scopus 로고    scopus 로고
    • Self-diffusion and cooperative diffusion of globular proteins in solution
    • Le Bon, C.; Nicolai, T.; Kuil, M. E.; Hollander, J. G. Self-diffusion and cooperative diffusion of globular proteins in solution. J. Phys. Chem. B 1999, 103, 10294-10299.
    • (1999) J. Phys. Chem. B , vol.103 , pp. 10294-10299
    • Le Bon, C.1    Nicolai, T.2    Kuil, M.E.3    Hollander, J.G.4
  • 38
    • 84974034558 scopus 로고
    • Low resolution NMR spectroscopy: A tool to study protein denaturation. I. Application to diamagnetic whey proteins
    • Lambelet, P.; Berrocal, R.; Ducret, F. Low resolution NMR spectroscopy: a tool to study protein denaturation. I. Application to diamagnetic whey proteins. J. Dairy. Sci. 1989, 56, 211-222.
    • (1989) J. Dairy. Sci. , vol.56 , pp. 211-222
    • Lambelet, P.1    Berrocal, R.2    Ducret, F.3
  • 39
    • 0030928138 scopus 로고    scopus 로고
    • Constant gradient stimulated echo studies of diffusion in porous materials at high spectrometer fields
    • Snaar, J. E. M.; Hills, B. P. Constant gradient stimulated echo studies of diffusion in porous materials at high spectrometer fields. Magn. Reson. Imaging 1997, 15, 983-992.
    • (1997) Magn. Reson. Imaging , vol.15 , pp. 983-992
    • Snaar, J.E.M.1    Hills, B.P.2
  • 40
    • 0036468090 scopus 로고    scopus 로고
    • Aggregation, gelation and phase separation of heat denatured globular proteins
    • Durand, D.; Gimel, J. C.; Nicolai, T. Aggregation, gelation and phase separation of heat denatured globular proteins. Physica A 2002, 304, 253-265.
    • (2002) Physica A , vol.304 , pp. 253-265
    • Durand, D.1    Gimel, J.C.2    Nicolai, T.3
  • 41
    • 24344492524 scopus 로고    scopus 로고
    • Dynamic regimes and correlated structural dynamics in native and denatured alpha-lactalbumin
    • Bu, Z. M.; Cook, J.; Callaway, D. J. E. Dynamic regimes and correlated structural dynamics in native and denatured alpha-lactalbumin. Biophys. J. 2002, 82, 310A-310A.
    • (2002) Biophys. J. , vol.82
    • Bu, Z.M.1    Cook, J.2    Callaway, D.J.E.3
  • 42
    • 0041352838 scopus 로고    scopus 로고
    • Quantification of heat-induced casein-whey protein interactions in milk and its relation to gelation kinetics
    • Vasbinder, A. J.; Alting, A. C.; de Kruif, K. G. Quantification of heat-induced casein-whey protein interactions in milk and its relation to gelation kinetics. Colloids Surf. B 2003, 31, 115-123.
    • (2003) Colloids Surf. B , vol.31 , pp. 115-123
    • Vasbinder, A.J.1    Alting, A.C.2    De Kruif, K.G.3
  • 43
    • 0142123418 scopus 로고    scopus 로고
    • Characterization of soluble aggregates from whey protein isolate
    • Kazmierski, M.; Corredig, M. Characterization of soluble aggregates from whey protein isolate. Food Hydrocolloids 2003, 17, 685-692.
    • (2003) Food Hydrocolloids , vol.17 , pp. 685-692
    • Kazmierski, M.1    Corredig, M.2
  • 44
    • 0000604267 scopus 로고
    • Physico-chemical and functional properties of milk proteins
    • Fox, F. H. J., Ed.; Elsevier Applied Science: London
    • Mulvihill, D. M.; Fox, F. H. J. Physico-chemical and functional properties of milk proteins. In Functional Milk Protein; Fox, F. H. J., Ed.; Elsevier Applied Science: London, 1989; pp 131-172.
    • (1989) Functional Milk Protein , pp. 131-172
    • Mulvihill, D.M.1    Fox, F.H.J.2
  • 45
    • 0000566482 scopus 로고    scopus 로고
    • Characterization of microemulsions by NMR
    • Kumar, P., Mittal, K. L., Eds.; Marcel Dekker: New York
    • Lindman, B.; Olsson, U.; Soderman, O. Characterization of microemulsions by NMR. In Handbook of Microemulsion Science and Technology; Kumar, P., Mittal, K. L., Eds.; Marcel Dekker: New York, 1999; pp 309-356.
    • (1999) Handbook of Microemulsion Science and Technology , pp. 309-356
    • Lindman, B.1    Olsson, U.2    Soderman, O.3
  • 46
    • 33751500335 scopus 로고
    • Self-diffusion in nonionic surfactant-water systems
    • Jonströmer, M.; Jönsson, B.; Lindman, B. Self-diffusion in nonionic surfactant-water systems. J. Phys. Chem. 1991, 95, 3291-3300.
    • (1991) J. Phys. Chem. , vol.95 , pp. 3291-3300
    • Jonströmer, M.1    Jönsson, B.2    Lindman, B.3


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