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Volumn 52, Issue 17, 2004, Pages 5449-5455

1H nuclear magnetic resonance relaxometry study of water state in milk protein mixtures

Author keywords

Casein; Hydration water; Lactose; NMR relaxation; pH effect

Indexed keywords

CALCIUM CHLORIDE; CASEIN; LACTOSE; MILK PROTEIN; PROTON; WATER; WHEY PROTEIN;

EID: 4143144372     PISSN: 00218561     EISSN: None     Source Type: Journal    
DOI: 10.1021/jf030777m     Document Type: Article
Times cited : (44)

References (50)
  • 1
    • 0022513002 scopus 로고
    • Water sorption by proteins: Milk and whey proteins
    • Kinsella, J. E.; Fox, P. F. Water sorption by proteins: milk and whey proteins. Crit. Rev. Food Sci. Nutr. 1986, 24, 91-139.
    • (1986) Crit. Rev. Food Sci. Nutr. , vol.24 , pp. 91-139
    • Kinsella, J.E.1    Fox, P.F.2
  • 3
    • 4143049930 scopus 로고    scopus 로고
    • L'eau dans les produits laitiers
    • Meste, M. L., Lorient, D., Simatos, D., Eds.; Editions Tec & Doc: Paris, France
    • Banon, S.; Hardy, J. L'eau dans les produits laitiers. In L'eau dans les Aliments; Meste, M. L., Lorient, D., Simatos, D., Eds.; Editions Tec & Doc: Paris, France, 2002; pp 235-255.
    • (2002) L'eau dans les Aliments , pp. 235-255
    • Banon, S.1    Hardy, J.2
  • 4
    • 0005964694 scopus 로고
    • Hydration of native and rennin coagulated caseins as determined by differential scanning calorimetry and gravimetric sorption measurements
    • Ruegg, M.; Luscher, M.; Blanc, B. Hydration of native and rennin coagulated caseins as determined by differential scanning calorimetry and gravimetric sorption measurements. J. Dairy Sci. 1973, 57, 387-393.
    • (1973) J. Dairy Sci. , vol.57 , pp. 387-393
    • Ruegg, M.1    Luscher, M.2    Blanc, B.3
  • 5
    • 0021663774 scopus 로고
    • Milk proteins: Physicochemical and functional properties
    • Kinsella, J. E. Milk proteins: physicochemical and functional properties. Crit. Rev. Food Sci. Nutr. 1984, 21, 197-262.
    • (1984) Crit. Rev. Food Sci. Nutr. , vol.21 , pp. 197-262
    • Kinsella, J.E.1
  • 8
    • 0025310597 scopus 로고
    • A new interpretation of proton NMR relaxation time measurements of water in food
    • Hills, B. P.; Takacs, S. F. 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
  • 9
    • 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
  • 11
    • 0032867252 scopus 로고    scopus 로고
    • 2: Physicochemical characteristics of micelles and rennet coagulation
    • 2: Physicochemical characteristics of micelles and rennet coagulation. Int. Dairy J. 1999, 9, 293-297.
    • (1999) Int. Dairy J. , vol.9 , pp. 293-297
    • Famelart, M.H.1    Le Graet, Y.2    Raulot, K.3
  • 12
    • 0032876078 scopus 로고    scopus 로고
    • On the self-assembly of sodium caseinate
    • Farrer, D.; Lips, A. On the self-assembly of sodium caseinate. Int. Dairy J. 1999, 9, 281-286.
    • (1999) Int. Dairy J. , vol.9 , pp. 281-286
    • Farrer, D.1    Lips, A.2
  • 13
    • 2342542293 scopus 로고    scopus 로고
    • NMR relaxometry and MRI for food quality control: Application to dairy products and processes
    • Webb, A., Belton, P. S., Gill, A. M., Rutledge, D. N., Eds.; Royal Society of Chemistry: Cambridge, U.K.
    • Mariette, F. NMR relaxometry and MRI for food quality control: application to dairy products and processes. In Magnetic Resonance in Food Science: Latest Developments; Webb, A., Belton, P. S., Gill, A. M., Rutledge, D. N., Eds.; Royal Society of Chemistry: Cambridge, U.K., 2003; p 209.
    • (2003) Magnetic Resonance in Food Science: Latest Developments , pp. 209
    • Mariette, F.1
  • 15
    • 84991140722 scopus 로고
    • A pulsed low resolution NMR study of water binding to powdered milk
    • Brosio, E.; Altobelli, G.; Yun Yu, S.; Di Nola, A. A pulsed low resolution NMR study of water binding to powdered milk. J. Food Technol. 1983, 18, 219-226.
    • (1983) J. Food Technol. , vol.18 , pp. 219-226
    • Brosio, E.1    Altobelli, G.2    Yun Yu, S.3    Di Nola, A.4
  • 17
    • 0036189112 scopus 로고    scopus 로고
    • Rehydration of casein powders: Effects of added mineral salts and salt addition methods on water transfer
    • Schuck, P.; Davenel, A.; Mariette, F.; Briard, V.; Mejean, S.; Piot, M. Rehydration of casein powders: Effects of added mineral salts and salt addition methods on water transfer. Int. Dairy J. 2002, 12, 51-57.
    • (2002) Int. Dairy J. , vol.12 , pp. 51-57
    • Schuck, P.1    Davenel, A.2    Mariette, F.3    Briard, V.4    Mejean, S.5    Piot, M.6
  • 18
    • 0035560071 scopus 로고    scopus 로고
    • Assessment of the state of water in reconstituted milk protein dispersions by nuclear magnetic resonance (NMR) and differential scanning calorimetry (DSC)
    • Le Dean, A.; Mariette, F.; Lucas, T.; Marin, M. Assessment of the state of water in reconstituted milk protein dispersions by nuclear magnetic resonance (NMR) and differential scanning calorimetry (DSC). Lebensm.-Wiss.-Technol. 2001, 34, 299-305.
    • (2001) Lebensm.-Wiss.-Technol. , vol.34 , pp. 299-305
    • Le Dean, A.1    Mariette, F.2    Lucas, T.3    Marin, M.4
  • 19
    • 85005586766 scopus 로고
    • A pulsed low-resolution NMR study of water binding to milk proteins
    • Brosio, E.; Altobelli, G.; Di Nola, A. A pulsed low-resolution NMR study of water binding to milk proteins. J. Food Technol. 1984, 19, 103-108.
    • (1984) J. Food Technol. , vol.19 , pp. 103-108
    • Brosio, E.1    Altobelli, G.2    Di Nola, A.3
  • 20
    • 0001744492 scopus 로고
    • Water interactions with bovine caseins by hydrogen-2 nuclear relaxation studies: Structural implications
    • Farrell, H. M. J.; Pessen, H.; Kumosinski, T. F. Water interactions with bovine caseins by hydrogen-2 nuclear relaxation studies: Structural implications. J. Dairy Sci. 1989, 72, 562-574.
    • (1989) J. Dairy Sci. , vol.72 , pp. 562-574
    • Farrell, H.M.J.1    Pessen, H.2    Kumosinski, T.F.3
  • 22
    • 33751154411 scopus 로고
    • Comparison of hydration behavior of bovine and caprine caseins as determined by oxygen-17 nuclear magnetic resonance: Effects of salt
    • Mora-Gutierrez, A.; Farrell, H. M.; Kumosinski, T. F. Comparison of hydration behavior of bovine and caprine caseins as determined by oxygen-17 nuclear magnetic resonance: effects of salt. J. Agric. Food Chem. 1995, 43, 2574-2579.
    • (1995) J. Agric. Food Chem. , vol.43 , pp. 2574-2579
    • Mora-Gutierrez, A.1    Farrell, H.M.2    Kumosinski, T.F.3
  • 23
    • 0002331909 scopus 로고    scopus 로고
    • Comparison of hydration behavior of bovine and caprine caseins as determined by oxygen-17 nuclear magnetic resonance: Temperature dependence of colloidal stability
    • Mora-Gutierrez, A.; Farrell, H. M.; Kumosinski, T. F. Comparison of hydration behavior of bovine and caprine caseins as determined by oxygen-17 nuclear magnetic resonance: Temperature dependence of colloidal stability. J. Agric. Food Chem. 1996, 44, 48-53.
    • (1996) J. Agric. Food Chem. , vol.44 , pp. 48-53
    • Mora-Gutierrez, A.1    Farrell, H.M.2    Kumosinski, T.F.3
  • 24
    • 0002331911 scopus 로고    scopus 로고
    • Comparison of hydration behavior of bovine and caprine caseins as determined by oxygen-17 nuclear magnetic resonance: pH/pD Dependence
    • Mora-Gutierrez, A.; Farrell, H. M.; Kumosinski, T. F. Comparison of hydration behavior of bovine and caprine caseins as determined by oxygen-17 nuclear magnetic resonance: pH/pD Dependence. J. Agric. Food Chem. 1996, 44, 796-803.
    • (1996) J. Agric. Food Chem. , vol.44 , pp. 796-803
    • Mora-Gutierrez, A.1    Farrell, H.M.2    Kumosinski, T.F.3
  • 25
    • 84971724964 scopus 로고
    • Low-field nuclear magnetic resonance relaxation study of thermal effects on milk proteins
    • Lambelet, P.; Berrocal, R.; Renevey, F. Low-field nuclear magnetic resonance relaxation study of thermal effects on milk proteins. J. Dairy Res. 1992, 59, 517-526.
    • (1992) J. Dairy Res. , vol.59 , pp. 517-526
    • Lambelet, P.1    Berrocal, R.2    Renevey, F.3
  • 26
    • 0033857440 scopus 로고    scopus 로고
    • Sugar-casein interaction in deuterated solutions of bovine and caprine casein as determined by oxygen-17 and carbon-13 nuclear magnetic resonance: A case of preferential interactions
    • Mora-Gutierrez, A.; Farrell, H. M. Sugar-casein interaction in deuterated solutions of bovine and caprine casein as determined by oxygen-17 and carbon-13 nuclear magnetic resonance: A case of preferential interactions. J. Agric. Food Chem. 2000, 48, 3245-3255.
    • (2000) J. Agric. Food Chem. , vol.48 , pp. 3245-3255
    • Mora-Gutierrez, A.1    Farrell, H.M.2
  • 27
    • 0642333026 scopus 로고    scopus 로고
    • Oxygen-17 nuclear magnetic resonance studies of bovine and caprine casein hydration and activity in deuterated sugar solutions
    • Mora-Guttierez, A.; Kumosinski, F.; Farrell, H. M. J. Oxygen-17 nuclear magnetic resonance studies of bovine and caprine casein hydration and activity in deuterated sugar solutions. J. Agric. Food Chem. 1997, 45, 4545-4553.
    • (1997) J. Agric. Food Chem. , vol.45 , pp. 4545-4553
    • Mora-Guttierez, A.1    Kumosinski, F.2    Farrell, H.M.J.3
  • 28
    • 0030492742 scopus 로고    scopus 로고
    • pH-induced physicochemical modifications of native phosphocaseinate suspensions: Influence of aqueous phase
    • Famelart, M. H.; Lepesant, F.; Gaucheron, F.; Legraet, Y.; Schuck, P. pH-induced physicochemical modifications of native phosphocaseinate suspensions: Influence of aqueous phase. Lait 1996, 76, 445-460.
    • (1996) Lait , vol.76 , pp. 445-460
    • Famelart, M.H.1    Lepesant, F.2    Gaucheron, F.3    Legraet, Y.4    Schuck, P.5
  • 29
    • 84974306858 scopus 로고
    • Study of acid milk coagulation by an optical method using light reflection
    • Banon, S.; Hardy, J. Study of acid milk coagulation by an optical method using light reflection. J. Dairy Res. 1991, 58, 75-84.
    • (1991) J. Dairy Res. , vol.58 , pp. 75-84
    • Banon, S.1    Hardy, J.2
  • 30
    • 3743110554 scopus 로고    scopus 로고
    • Micellar transition state in casein between pH 5.5 and 5.0
    • Gastaldi, E.; Lagaude, A.; Delafuente, B. T. Micellar transition state in casein between pH 5.5 and 5.0. J. Food Sci. 1996, 61, 59-65.
    • (1996) J. Food Sci. , vol.61 , pp. 59-65
    • Gastaldi, E.1    Lagaude, A.2    Delafuente, B.T.3
  • 31
    • 49349118272 scopus 로고
    • The measurement of cross-relaxation effetcts in the proton NMR spin-lattice relaxation of water in biological systems: Hydrated collagen and muscle
    • Edzes, H. T.; Samulski, E. T. The measurement of cross-relaxation effetcts in the proton NMR spin-lattice relaxation of water in biological systems: Hydrated collagen and muscle. J. Magn. Reson. 1978, 31, 207-229.
    • (1978) J. Magn. Reson. , vol.31 , pp. 207-229
    • Edzes, H.T.1    Samulski, E.T.2
  • 32
    • 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
  • 33
    • 0014575738 scopus 로고
    • Investigation of proton relaxation in live plant tissues by the spin-echo method
    • Fedotov, V. D.; Miftakhutdinova, F. G.; Murtazin, F. Investigation of proton relaxation in live plant tissues by the spin-echo method. Biofizika 1969, 14, 873-882.
    • (1969) Biofizika , vol.14 , pp. 873-882
    • Fedotov, V.D.1    Miftakhutdinova, F.G.2    Murtazin, F.3
  • 34
    • 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
  • 35
    • 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
  • 36
    • 0000169232 scopus 로고
    • An algorithm for least squares estimations of nonlinear parameters
    • Marquardt, D. W. An algorithm for least squares estimations of nonlinear parameters. J. Soc. Ind. Appl. Math. 1963, 11, 431.
    • (1963) J. Soc. Ind. Appl. Math. , vol.11 , pp. 431
    • Marquardt, D.W.1
  • 37
    • 77956853420 scopus 로고    scopus 로고
    • Continuous relaxation time distribution decomposition by MEM
    • Rutledge, D. N., Ed.; Elsevier: Amsterdam, The Netherlands
    • Mariette, F.; Guillement, J. P.; Tellier, C.; Marchal, P. Continuous relaxation time distribution decomposition by MEM. In Signal Treatment and Signal Analysis in NMR; Rutledge, D. N., Ed.; Elsevier: Amsterdam, The Netherlands, 1996; pp 218-234.
    • (1996) Signal Treatment and Signal Analysis in NMR , pp. 218-234
    • Mariette, F.1    Guillement, J.P.2    Tellier, C.3    Marchal, P.4
  • 38
    • 0020199187 scopus 로고
    • A deuteron and proton magnetci resonance relaxation study of β-lactoglobulin A association: Some approaches to the scatchard hydration of globular proteins
    • Kumosinski, T. F.; Pessen, H. A deuteron and proton magnetci resonance relaxation study of β-lactoglobulin A association: Some approaches to the scatchard hydration of globular proteins. Arch. Biochem. Biophys. 1982, 218, 286-302.
    • (1982) Arch. Biochem. Biophys. , vol.218 , pp. 286-302
    • Kumosinski, T.F.1    Pessen, H.2
  • 39
    • 0031540994 scopus 로고    scopus 로고
    • A NMR relaxometry method for determining the reconstitutability and the water-holding capacity of protein-rich milk powders
    • Davenel, A.; Schuck, P.; Marchal, P. A NMR relaxometry method for determining the reconstitutability and the water-holding capacity of protein-rich milk powders. Milchwissenschaft - Milk Sci. Int. 1997, 52, 35-39.
    • (1997) Milchwissenschaft - Milk Sci. Int. , vol.52 , pp. 35-39
    • Davenel, A.1    Schuck, P.2    Marchal, P.3
  • 40
    • 85025797643 scopus 로고
    • On the stability of casein micelles
    • Walstra, P. On the stability of casein micelles. J. Dairy Sci. 1990, 73, 1968-1979.
    • (1990) J. Dairy Sci. , vol.73 , pp. 1968-1979
    • Walstra, P.1
  • 41
    • 84976088848 scopus 로고
    • pH-induced dissociation of bovine casein micelles. 2. Mineral solubilization and its relation to casein release
    • Dalgeish, D. G.; Law, J. R. pH-induced dissociation of bovine casein micelles. 2. Mineral solubilization and its relation to casein release. J. Dairy Res. 1989, 56, 727-735.
    • (1989) J. Dairy Res. , vol.56 , pp. 727-735
    • Dalgeish, D.G.1    Law, J.R.2
  • 42
    • 84971758074 scopus 로고
    • pH-induced dissociation of bovine casein micelles. 1. Analysis of liberated caseins
    • Dalgleish, D. G.; Law, A. J. R. pH-induced dissociation of bovine casein micelles. 1. Analysis of liberated caseins. J. Dairy Res. 1988, 55, 529-538.
    • (1988) J. Dairy Res. , vol.55 , pp. 529-538
    • Dalgleish, D.G.1    Law, A.J.R.2
  • 43
    • 0001558145 scopus 로고
    • pH-induced physico-chemical changes of casein micelles in milk and their effect on renneing. 1. Effect of acidification on physicochemical properties
    • Van Hooydonk, A. C. M.; Hagedoom, H. G.; Boerrigter, I. J. pH-induced physico-chemical changes of casein micelles in milk and their effect on renneing. 1. Effect of acidification on physicochemical properties. Neth. Milk Dairy J. 1986, 40, 281-296.
    • (1986) Neth. Milk Dairy J. , vol.40 , pp. 281-296
    • Van Hooydonk, A.C.M.1    Hagedoom, H.G.2    Boerrigter, I.J.3
  • 44
    • 0000027825 scopus 로고
    • Etude de la coagulation du lait par la presure et de la synerese du coagulum par la methode thromboelatographique
    • Tarodo de la Fuente, B.; Alais, C. Etude de la coagulation du lait par la presure et de la synerese du coagulum par la methode thromboelatographique. Lait 1969, 487, 400-415.
    • (1969) Lait , vol.487 , pp. 400-415
    • Tarodo De La Fuente, B.1    Alais, C.2
  • 45
    • 0028204808 scopus 로고
    • Application of spin-spin relaxation to measurement of surface area and pore size distributions in hydrating cement paste
    • Halperin, W. P.; Jehng, J. Y.; Song, Y. Q. Application of spin-spin relaxation to measurement of surface area and pore size distributions in hydrating cement paste. Magn. Reson. Imaging 1995, 12, 169-173.
    • (1995) Magn. Reson. Imaging , vol.12 , pp. 169-173
    • Halperin, W.P.1    Jehng, J.Y.2    Song, Y.Q.3
  • 46
    • 0025896727 scopus 로고
    • Water-protein interactions-theory and experiment
    • Teeter, M. M. Water-protein interactions-theory and experiment. Annu. Rev. Biophys. Biophys. Chem. 1991, 20, 577-600.
    • (1991) Annu. Rev. Biophys. Biophys. Chem. , vol.20 , pp. 577-600
    • Teeter, M.M.1
  • 47
    • 0036985541 scopus 로고    scopus 로고
    • Micellar casein gelation at high sucrose content
    • Schorsch, C.; Jones, M. G.; Norton, I. T. Micellar casein gelation at high sucrose content. J. Dairy Sci. 2002, 85, 3155-3163.
    • (2002) J. Dairy Sci. , vol.85 , pp. 3155-3163
    • Schorsch, C.1    Jones, M.G.2    Norton, I.T.3
  • 49
    • 0002215859 scopus 로고
    • Lactose: Chemical and physicochemical properties
    • Fox, P. F., Ed.; Elsevier Applied Science Publishers: Amsterdam, The Netherlands
    • Morissey, P. A. Lactose: chemical and physicochemical properties. In Developments in Dairy Chemistry-3 Lactose and Minor Constituents; Fox, P. F., Ed.; Elsevier Applied Science Publishers: Amsterdam, The Netherlands, 1985; pp 1-34.
    • (1985) Developments in Dairy Chemistry-3 Lactose and Minor Constituents , pp. 1-34
    • Morissey, P.A.1
  • 50
    • 4143137249 scopus 로고
    • Low-resolution, pulsed NMR studies of water binding and of exchangeable hydrogen content in solids
    • Brosio, E.; Conti, F.; Paci, M. Low-resolution, pulsed NMR studies of water binding and of exchangeable hydrogen content in solids. J. Magn. Reson. 1979, 34, 593-597.
    • (1979) J. Magn. Reson. , vol.34 , pp. 593-597
    • Brosio, E.1    Conti, F.2    Paci, M.3


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