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Volumn 95, Issue 4, 2012, Pages 1603-1616

Effect of temperature and pH on the solubility of caseins: Environmental influences on the dissociation of α S- and β-casein

Author keywords

casein; Calcium; Casein; Solubility

Indexed keywords

CALCIUM; CALCIUM CASEINATE; CASEIN; WATER;

EID: 84858954599     PISSN: 00220302     EISSN: 15253198     Source Type: Journal    
DOI: 10.3168/jds.2011-4641     Document Type: Article
Times cited : (127)

References (77)
  • 1
    • 55249108994 scopus 로고    scopus 로고
    • Physico-chemical characteristics of casein micelles from buffalo milk in different ionic environments: A comparison with cow milk
    • Ahmad S., Rousseau F., Grongnet J.F., Gaucheron F. Physico-chemical characteristics of casein micelles from buffalo milk in different ionic environments: A comparison with cow milk. Milchwissenschaft 2008, 63:390-393.
    • (2008) Milchwissenschaft , vol.63 , pp. 390-393
    • Ahmad, S.1    Rousseau, F.2    Grongnet, J.F.3    Gaucheron, F.4
  • 2
    • 85032070238 scopus 로고
    • Factors influencing casein distribution in cold-stored milk and their effects on cheese-making parameters
    • Ali A.E., Andrews A.T., Cheeseman G.C. Factors influencing casein distribution in cold-stored milk and their effects on cheese-making parameters. J. Dairy Res. 1980, 47:383-391.
    • (1980) J. Dairy Res. , vol.47 , pp. 383-391
    • Ali, A.E.1    Andrews, A.T.2    Cheeseman, G.C.3
  • 3
    • 0030186201 scopus 로고    scopus 로고
    • ζ-Potentials of casein micelles from reconstituted skim milk heated at 120°C
    • Anema S.G., Klostermeyer H. ζ-Potentials of casein micelles from reconstituted skim milk heated at 120°C. Int. Dairy J. 1996, 6:673-687.
    • (1996) Int. Dairy J. , vol.6 , pp. 673-687
    • Anema, S.G.1    Klostermeyer, H.2
  • 5
    • 85010253174 scopus 로고
    • Interaction of casein components as measured by turbidity
    • Ashworth U.S. Interaction of casein components as measured by turbidity. J. Dairy Sci. 1964, 47:351-355.
    • (1964) J. Dairy Sci. , vol.47 , pp. 351-355
    • Ashworth, U.S.1
  • 6
    • 0034373708 scopus 로고    scopus 로고
    • Mineral salts and their effect on milk functionality
    • Augustin M.A. Mineral salts and their effect on milk functionality. Aust. J. Dairy Technol. 2000, 55:61-64.
    • (2000) Aust. J. Dairy Technol. , vol.55 , pp. 61-64
    • Augustin, M.A.1
  • 8
    • 24244438505 scopus 로고
    • s1-, β- and κ-casein
    • s1-, β- and κ-casein. J. Dairy Sci. 1971, 54:1077-1080.
    • (1971) J. Dairy Sci. , vol.54 , pp. 1077-1080
    • Bingham, E.W.1
  • 9
    • 41949085890 scopus 로고    scopus 로고
    • Impact of zeta potential and size of caseins as precursors of fouling deposit on limiting and critical fluxes in spiral ultrafiltration of modified skim milks
    • Bouzid H., Rabiller-Baudry M., Paugam L., Rousseau F., Derriche Z., Bettahar N.E. Impact of zeta potential and size of caseins as precursors of fouling deposit on limiting and critical fluxes in spiral ultrafiltration of modified skim milks. J. Membr. Sci. 2008, 314:67-75.
    • (2008) J. Membr. Sci. , vol.314 , pp. 67-75
    • Bouzid, H.1    Rabiller-Baudry, M.2    Paugam, L.3    Rousseau, F.4    Derriche, Z.5    Bettahar, N.E.6
  • 10
    • 0034199281 scopus 로고    scopus 로고
    • Bioactive milk peptides: A prospectus
    • Clare D.A., Swaisgood H.E. Bioactive milk peptides: A prospectus. J. Dairy Sci. 2000, 83:1187-1195.
    • (2000) J. Dairy Sci. , vol.83 , pp. 1187-1195
    • Clare, D.A.1    Swaisgood, H.E.2
  • 11
    • 0015518523 scopus 로고
    • Hydrogen ion equilibria of bovine β-casein-B
    • Creamer L.K. Hydrogen ion equilibria of bovine β-casein-B. Biochim. Biophys. Acta 1972, 271:252-261.
    • (1972) Biochim. Biophys. Acta , vol.271 , pp. 252-261
    • Creamer, L.K.1
  • 12
    • 0001400692 scopus 로고
    • Measurement of electrophoretic mobilities and zeta-potentials of particles from milk using laser Doppler electrophoresis
    • Dalgleish D.G. Measurement of electrophoretic mobilities and zeta-potentials of particles from milk using laser Doppler electrophoresis. J. Dairy Res. 1984, 51:425-438.
    • (1984) J. Dairy Res. , vol.51 , pp. 425-438
    • Dalgleish, D.G.1
  • 13
    • 84971758074 scopus 로고
    • PH-induced dissociation of bovine casein micelles. I. Analysis of liberated caseins
    • Dalgleish D.G., Law A.J.R. pH-induced dissociation of bovine casein micelles. I. 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
  • 14
    • 84976088848 scopus 로고
    • PH-Induced dissociation of bovine casein micelles. II. Mineral solubilization and its relation to casein release
    • Dalgleish D.G., Law A.J.R. pH-Induced dissociation of bovine casein micelles. II. Mineral solubilization and its relation to casein release. J. Dairy Res. 1989, 56:727-735.
    • (1989) J. Dairy Res. , vol.56 , pp. 727-735
    • Dalgleish, D.G.1    Law, A.J.R.2
  • 16
    • 33747200222 scopus 로고    scopus 로고
    • Structure formation in casein-based gels, foams, and emulsions
    • Dickinson E. Structure formation in casein-based gels, foams, and emulsions. Colloids Surf. 2006, 288:3-11.
    • (2006) Colloids Surf. , vol.288 , pp. 3-11
    • Dickinson, E.1
  • 17
  • 18
    • 85006697969 scopus 로고
    • 2 caseins and their stabilization by κ-casein A
    • 2 caseins and their stabilization by κ-casein A. J. Dairy Sci. 1976, 59:203-206.
    • (1976) J. Dairy Sci. , vol.59 , pp. 203-206
    • Eigel, W.N.1    Randolph, H.E.2
  • 19
    • 12344310391 scopus 로고    scopus 로고
    • Simulating the self-association of caseins
    • Euston S.R., Horne D.S. Simulating the self-association of caseins. Food Hydrocoll. 2005, 19:379-386.
    • (2005) Food Hydrocoll. , vol.19 , pp. 379-386
    • Euston, S.R.1    Horne, D.S.2
  • 20
    • 84985278900 scopus 로고
    • Caseinate at low temperatures: Calcium use in β-casein extraction by microfiltration
    • Famelart M.H., Surel O. Caseinate at low temperatures: Calcium use in β-casein extraction by microfiltration. J. Food Sci. 1994, 59:548-553.
    • (1994) J. Food Sci. , vol.59 , pp. 548-553
    • Famelart, M.H.1    Surel, O.2
  • 22
    • 0542415083 scopus 로고
    • Modeling of calcium-induced solubility profiles of casein for biotechnology: Influence of primary structure and posttranslational modification
    • Farrell H.M., Kumosinski T.F. Modeling of calcium-induced solubility profiles of casein for biotechnology: Influence of primary structure and posttranslational modification. J. Ind. Microbiol. 1988, 3:61-71.
    • (1988) J. Ind. Microbiol. , vol.3 , pp. 61-71
    • Farrell, H.M.1    Kumosinski, T.F.2
  • 24
    • 0023735079 scopus 로고
    • Calcium-induced associations of the caseins: A thermodynamic linkage approach to precipitation and resolubilization
    • Farrell H.M.J., Kumosinski T.F., Pulaski P., Thompson M.P. Calcium-induced associations of the caseins: A thermodynamic linkage approach to precipitation and resolubilization. Arch. Biochem. Biophys. 1988, 265:146-158.
    • (1988) Arch. Biochem. Biophys. , vol.265 , pp. 146-158
    • Farrell, H.M.J.1    Kumosinski, T.F.2    Pulaski, P.3    Thompson, M.P.4
  • 25
    • 1842661636 scopus 로고    scopus 로고
    • Recovery of lactoferrin and lactoperoxidase from sweet whey using colloidal gas aphrons (CGAs) generated from an anionic surfactant, AOT
    • Fuda E., Jauregi P., Pyle D.L. Recovery of lactoferrin and lactoperoxidase from sweet whey using colloidal gas aphrons (CGAs) generated from an anionic surfactant, AOT. Biotechnol. Prog. 2004, 20:514-525.
    • (2004) Biotechnol. Prog. , vol.20 , pp. 514-525
    • Fuda, E.1    Jauregi, P.2    Pyle, D.L.3
  • 26
    • 44849107381 scopus 로고    scopus 로고
    • Characterisation of sodium caseinate as a function of ionic strength, pH and temperature using static and dynamic light scattering
    • HadjSadok A., Pitkowski A., Nicolai T., Benyahia L., Moulai-Mostefa N. Characterisation of sodium caseinate as a function of ionic strength, pH and temperature using static and dynamic light scattering. Food Hydrocoll. 2008, 22:1460-1466.
    • (2008) Food Hydrocoll. , vol.22 , pp. 1460-1466
    • HadjSadok, A.1    Pitkowski, A.2    Nicolai, T.3    Benyahia, L.4    Moulai-Mostefa, N.5
  • 28
    • 0026668858 scopus 로고
    • Structure and stability of bovine casein micelles
    • Holt C. Structure and stability of bovine casein micelles. Adv. Protein Chem. 1992, 43:63-151.
    • (1992) Adv. Protein Chem. , vol.43 , pp. 63-151
    • Holt, C.1
  • 29
    • 0032029213 scopus 로고    scopus 로고
    • Casein interactions: Casting light on the black boxes, the structure in dairy products
    • Horne D.S. Casein interactions: Casting light on the black boxes, the structure in dairy products. Int. Dairy J. 1998, 8:171-177.
    • (1998) Int. Dairy J. , vol.8 , pp. 171-177
    • Horne, D.S.1
  • 31
    • 33744979970 scopus 로고    scopus 로고
    • Effect of NaCl on some physico-chemical properties of concentrated bovine milk
    • Huppertz T., Fox P.F. Effect of NaCl on some physico-chemical properties of concentrated bovine milk. Int. Dairy J. 2006, 16:1142-1148.
    • (2006) Int. Dairy J. , vol.16 , pp. 1142-1148
    • Huppertz, T.1    Fox, P.F.2
  • 33
    • 43049111426 scopus 로고    scopus 로고
    • Reformation of casein particles from alkaline-disrupted casein micelles
    • Huppertz T., Vaia B., Smiddy M.A. Reformation of casein particles from alkaline-disrupted casein micelles. J. Dairy Res. 2008, 75:44-47.
    • (2008) J. Dairy Res. , vol.75 , pp. 44-47
    • Huppertz, T.1    Vaia, B.2    Smiddy, M.A.3
  • 34
    • 0033868551 scopus 로고    scopus 로고
    • Soluble protein fractions from pH and heat treated sodium caseinate: physicochemical and functional properties
    • Jahaniaval F., Kakuda Y., Abraham V., Marcone M.F. Soluble protein fractions from pH and heat treated sodium caseinate: physicochemical and functional properties. Food Res. Int. 2000, 33:637-647.
    • (2000) Food Res. Int. , vol.33 , pp. 637-647
    • Jahaniaval, F.1    Kakuda, Y.2    Abraham, V.3    Marcone, M.F.4
  • 35
    • 0037898041 scopus 로고    scopus 로고
    • Proteinfraktionierung mittels Membrantrennverfahren [Protein fractionation by means of membrane processing]
    • PhD Thesis. Technical University of Munich, Munich, Germany.
    • Kersten, M. 2001. Proteinfraktionierung mittels Membrantrennverfahren [Protein fractionation by means of membrane processing]. PhD Thesis. Technical University of Munich, Munich, Germany.
    • (2001)
    • Kersten, M.1
  • 36
    • 2142678065 scopus 로고    scopus 로고
    • Peptides from milk proteins and their properties
    • Kilara A., Panyam D. Peptides from milk proteins and their properties. Crit. Rev. Food Sci. Nutr. 2003, 43:607-633.
    • (2003) Crit. Rev. Food Sci. Nutr. , vol.43 , pp. 607-633
    • Kilara, A.1    Panyam, D.2
  • 37
    • 64049107900 scopus 로고    scopus 로고
    • Bioactive milk proteins and peptides: From science to functional applications
    • Korhonen H.J. Bioactive milk proteins and peptides: From science to functional applications. Aust. J. Dairy Technol. 2009, 64:16-25.
    • (2009) Aust. J. Dairy Technol. , vol.64 , pp. 16-25
    • Korhonen, H.J.1
  • 38
    • 37149052697 scopus 로고    scopus 로고
    • Short communication: Extraction of β-casein from goat milk
    • Lamothe S., Robitaille G., St-Gelais D., Britten M. Short communication: Extraction of β-casein from goat milk. J. Dairy Sci. 2007, 90:5380-5382.
    • (2007) J. Dairy Sci. , vol.90 , pp. 5380-5382
    • Lamothe, S.1    Robitaille, G.2    St-Gelais, D.3    Britten, M.4
  • 39
    • 0001192135 scopus 로고    scopus 로고
    • Effects of heat treatment and acidification on the dissociation of bovine casein micelles
    • Law A.J.R. Effects of heat treatment and acidification on the dissociation of bovine casein micelles. J. Dairy Res. 1996, 63:35-48.
    • (1996) J. Dairy Res. , vol.63 , pp. 35-48
    • Law, A.J.R.1
  • 40
    • 0000702316 scopus 로고    scopus 로고
    • Effects of acidification and storage of milk on dissociation of bovine casein micelles
    • Law A.J.R., Leaver J. Effects of acidification and storage of milk on dissociation of bovine casein micelles. J. Agric. Food Chem. 1998, 46:5008-5016.
    • (1998) J. Agric. Food Chem. , vol.46 , pp. 5008-5016
    • Law, A.J.R.1    Leaver, J.2
  • 41
    • 33751252924 scopus 로고    scopus 로고
    • inventors. Methods of extracting casein fractions from milk and caseinates and production of novel products
    • Hanna Research Institute, assignee. WO Pat. No. 03003847.
    • Law, A. J. R. and J. Leaver, inventors 2007. Methods of extracting casein fractions from milk and caseinates and production of novel products. Hanna Research Institute, assignee. WO Pat. No. 03003847.
    • (2007)
    • Law, A.J.R.1    Leaver, J.2
  • 42
    • 0028389112 scopus 로고
    • Fouling and selectivity of membranes during separation of β-casein
    • Le Berre O., Daufin G. Fouling and selectivity of membranes during separation of β-casein. J. Membr. Sci. 1994, 88:263-270.
    • (1994) J. Membr. Sci. , vol.88 , pp. 263-270
    • Le Berre, O.1    Daufin, G.2
  • 43
    • 84858991523 scopus 로고
    • inventors. Method for obtaining beta-casein. Eurial-Parc Club du Perray, assignee
    • US Pat. No. 5397577.
    • Le Magnen, C., and J.-J. Maugas, inventors. 1995. Method for obtaining beta-casein. Eurial-Parc Club du Perray, assignee. US Pat. No. 5397577.
    • (1995)
    • Le Magnen, C.1    Maugas, J.-J.2
  • 44
    • 0001183694 scopus 로고
    • Structural and functional properties of caseinate and whey protein isolate as affected by temperature and pH
    • Lee S.-Y., Morr C.V., Ha E.Y.W. Structural and functional properties of caseinate and whey protein isolate as affected by temperature and pH. J. Food Sci. 1992, 57:1210-1229.
    • (1992) J. Food Sci. , vol.57 , pp. 1210-1229
    • Lee, S.-Y.1    Morr, C.V.2    Ha, E.Y.W.3
  • 45
    • 46049093569 scopus 로고    scopus 로고
    • PH-dependent structures and properties of casein micelles
    • Liu Y., Guo R. pH-dependent structures and properties of casein micelles. Biophys. Chem. 2008, 136:67-73.
    • (2008) Biophys. Chem. , vol.136 , pp. 67-73
    • Liu, Y.1    Guo, R.2
  • 46
    • 0030097893 scopus 로고    scopus 로고
    • Effect of acidification and neutralization of milk on some physico-chemical properties of casein micelles
    • Lucey J.A., Gorry C., O'Kennedy B., Kalab M., Tan-Kinita R., Fox P.F. Effect of acidification and neutralization of milk on some physico-chemical properties of casein micelles. Int. Dairy J. 1996, 6:257-272.
    • (1996) Int. Dairy J. , vol.6 , pp. 257-272
    • Lucey, J.A.1    Gorry, C.2    O'Kennedy, B.3    Kalab, M.4    Tan-Kinita, R.5    Fox, P.F.6
  • 47
    • 66149106351 scopus 로고    scopus 로고
    • Sodium caseinates with an altered isoelectric point as emulsifiers in oil/water systems
    • Ma H., Forssell P., Partanen R., Seppänen R., Buchert J., Boer H. Sodium caseinates with an altered isoelectric point as emulsifiers in oil/water systems. J. Agric. Food Chem. 2009, 57:3800-3807.
    • (2009) J. Agric. Food Chem. , vol.57 , pp. 3800-3807
    • Ma, H.1    Forssell, P.2    Partanen, R.3    Seppänen, R.4    Buchert, J.5    Boer, H.6
  • 50
    • 36649033587 scopus 로고    scopus 로고
    • Importance of intrinsic properties of dense caseinate dispersions for structure formation
    • Manski J.M., van Riemsdijk L.E., van der Goot A.J., Boom R.M. Importance of intrinsic properties of dense caseinate dispersions for structure formation. Biomacromolecules 2007, 8:3540-3547.
    • (2007) Biomacromolecules , vol.8 , pp. 3540-3547
    • Manski, J.M.1    van Riemsdijk, L.E.2    van der Goot, A.J.3    Boom, R.M.4
  • 51
    • 0030749136 scopus 로고    scopus 로고
    • Biochemical properties of regulatory peptides derived from milk proteins
    • Meisel H. Biochemical properties of regulatory peptides derived from milk proteins. Biopolymers 1997, 43:119-128.
    • (1997) Biopolymers , vol.43 , pp. 119-128
    • Meisel, H.1
  • 52
    • 33846980153 scopus 로고    scopus 로고
    • Physicochemical analysis of casein solubility in water-ethanol solutions
    • Mezdour S., Brulé G., Korolczuk J. Physicochemical analysis of casein solubility in water-ethanol solutions. Lait 2006, 86:435-452.
    • (2006) Lait , vol.86 , pp. 435-452
    • Mezdour, S.1    Brulé, G.2    Korolczuk, J.3
  • 53
    • 42249101607 scopus 로고    scopus 로고
    • Effect of temperature on self-assembly of bovine β-casein above and below isoelectric pH. Structural analysis by cryogenic-transmission electron microscopy and small-angle X-ray scattering
    • Moitzi C., Portnaya I., Glatter O., Ramon O., Danino D. Effect of temperature on self-assembly of bovine β-casein above and below isoelectric pH. Structural analysis by cryogenic-transmission electron microscopy and small-angle X-ray scattering. Langmuir 2008, 24:3020-3029.
    • (2008) Langmuir , vol.24 , pp. 3020-3029
    • Moitzi, C.1    Portnaya, I.2    Glatter, O.3    Ramon, O.4    Danino, D.5
  • 54
    • 0025917556 scopus 로고
    • Fractionation of sodium caseinate by ultrafiltration
    • Murphy J.M., Fox P.F. Fractionation of sodium caseinate by ultrafiltration. Food Chem. 1991, 39:27-38.
    • (1991) Food Chem. , vol.39 , pp. 27-38
    • Murphy, J.M.1    Fox, P.F.2
  • 57
    • 84858968305 scopus 로고    scopus 로고
    • inventors. Purification of β-casein from milk
    • US Pat. No. 0104847 A1.
    • O'Mahony, J. A., K. E. Smith, and J. A. Lucey, inventors. 2007. Purification of β-casein from milk. US Pat. No. 0104847 A1.
    • (2007)
    • O'Mahony, J.A.1    Smith, K.E.2    Lucey, J.A.3
  • 58
    • 0019525601 scopus 로고
    • Binding of calcium ions to bovine β-casein
    • Parker T.G., Dalgleish D.G. Binding of calcium ions to bovine β-casein. J. Dairy Res. 1981, 48:71-76.
    • (1981) J. Dairy Res. , vol.48 , pp. 71-76
    • Parker, T.G.1    Dalgleish, D.G.2
  • 59
    • 69349102184 scopus 로고    scopus 로고
    • Casein-derived bioactive peptides: Biological effects, industrial uses, safety aspects and regulatory status
    • Phelan M., Aherne A., FitzGerald R.J., O'Brien N.M. Casein-derived bioactive peptides: Biological effects, industrial uses, safety aspects and regulatory status. Int. Dairy J. 2009, 19:643-654.
    • (2009) Int. Dairy J. , vol.19 , pp. 643-654
    • Phelan, M.1    Aherne, A.2    FitzGerald, R.J.3    O'Brien, N.M.4
  • 60
    • 57849151119 scopus 로고    scopus 로고
    • Stability of caseinate solutions in the presence of calcium
    • Pitkowski A., Nicolai T., Durand D. Stability of caseinate solutions in the presence of calcium. Food Hydrocoll. 2009, 23:1164-1168.
    • (2009) Food Hydrocoll. , vol.23 , pp. 1164-1168
    • Pitkowski, A.1    Nicolai, T.2    Durand, D.3
  • 61
    • 63749103525 scopus 로고    scopus 로고
    • β-Casein as a bioactive precursor-Processing for purification
    • Post A.E., Ebert M., Hinrichs J. β-Casein as a bioactive precursor-Processing for purification. Aust. J. Dairy Technol. 2009, 64:84-88.
    • (2009) Aust. J. Dairy Technol. , vol.64 , pp. 84-88
    • Post, A.E.1    Ebert, M.2    Hinrichs, J.3
  • 62
    • 77951736259 scopus 로고    scopus 로고
    • Suitability of commercial caseinates in comparison to micellar casein as raw material for isolation of food-grade β-casein
    • Post A.E., Hinrichs J. Suitability of commercial caseinates in comparison to micellar casein as raw material for isolation of food-grade β-casein. Milchwissenschaft 2010, 65:195-198.
    • (2010) Milchwissenschaft , vol.65 , pp. 195-198
    • Post, A.E.1    Hinrichs, J.2
  • 63
    • 80055066475 scopus 로고    scopus 로고
    • Large-scale isolation of food-grade β-casein
    • Post A.E., Hinrichs J. Large-scale isolation of food-grade β-casein. Milchwissenschaft 2011, 66:361-364.
    • (2011) Milchwissenschaft , vol.66 , pp. 361-364
    • Post, A.E.1    Hinrichs, J.2
  • 64
    • 16644392534 scopus 로고    scopus 로고
    • Thermal and alkaline denaturation of bovine β-casein
    • Qi P.X., Wickham E.D., Farrell H.M. Thermal and alkaline denaturation of bovine β-casein. Protein J. 2004, 23:389-402.
    • (2004) Protein J. , vol.23 , pp. 389-402
    • Qi, P.X.1    Wickham, E.D.2    Farrell, H.M.3
  • 65
    • 23444460833 scopus 로고    scopus 로고
    • Limiting flux in skimmed milk ultrafiltration: Impact of electrostatic repulsion due to casein micelles
    • Rabiller-Baudry M., Gesan-Guiziou G., Roldan-Calbo D., Beaulieu S., Michel F. Limiting flux in skimmed milk ultrafiltration: Impact of electrostatic repulsion due to casein micelles. Desalination 2005, 175:49-59.
    • (2005) Desalination , vol.175 , pp. 49-59
    • Rabiller-Baudry, M.1    Gesan-Guiziou, G.2    Roldan-Calbo, D.3    Beaulieu, S.4    Michel, F.5
  • 66
    • 84935026369 scopus 로고
    • inventors. A process for producing beta-casein enriched products
    • New Zealand Dairy Research Institute, assignee. WO Pat. No. 006306.
    • Ram, S., D. W. Loh, D. C. Love, and P. D. Elston, inventors. 1994. A process for producing beta-casein enriched products. New Zealand Dairy Research Institute, assignee. WO Pat. No. 006306.
    • (1994)
    • Ram, S.1    Loh, D.W.2    Love, D.C.3    Elston, P.D.4
  • 67
    • 0034118944 scopus 로고    scopus 로고
    • Effect of storage at 4°C on the physicochemical and renneting properties of milk: A comparison of caprine, ovine and bovine milks
    • Raynal K., Remeuf F. Effect of storage at 4°C on the physicochemical and renneting properties of milk: A comparison of caprine, ovine and bovine milks. J. Dairy Res. 2000, 67:199-207.
    • (2000) J. Dairy Res. , vol.67 , pp. 199-207
    • Raynal, K.1    Remeuf, F.2
  • 68
    • 84971761380 scopus 로고
    • Relation between micellar and serum casein in bovine milk
    • Rose D. Relation between micellar and serum casein in bovine milk. J. Dairy Sci. 1968, 51:1897-1902.
    • (1968) J. Dairy Sci. , vol.51 , pp. 1897-1902
    • Rose, D.1
  • 69
    • 46149136490 scopus 로고
    • Effect of calcium on the hydration of casein. II. Binding of calcium chloride to whole casein and calcium caseinate
    • Rüegg M., Moor U. Effect of calcium on the hydration of casein. II. Binding of calcium chloride to whole casein and calcium caseinate. LWT-Food Sci. Technol. 1986, 19:386-391.
    • (1986) LWT-Food Sci. Technol. , vol.19 , pp. 386-391
    • Rüegg, M.1    Moor, U.2
  • 70
    • 8844258885 scopus 로고    scopus 로고
    • Caseins as source of bioactive peptides
    • Silva S.V., Malcata F.X. Caseins as source of bioactive peptides. Int. Dairy J. 2005, 15:1-15.
    • (2005) Int. Dairy J. , vol.15 , pp. 1-15
    • Silva, S.V.1    Malcata, F.X.2
  • 71
    • 0000504780 scopus 로고    scopus 로고
    • Sodium caseinate-stabilized emulsions: Factors affecting coverage and composition of surface proteins
    • Srinivasan M., Singh H., Munro P.A. Sodium caseinate-stabilized emulsions: Factors affecting coverage and composition of surface proteins. J. Agric. Food Chem. 1996, 44:3807-3811.
    • (1996) J. Agric. Food Chem. , vol.44 , pp. 3807-3811
    • Srinivasan, M.1    Singh, H.2    Munro, P.A.3
  • 72
    • 21344496774 scopus 로고
    • Effect of sodium chloride on the solubility of caseins
    • Strange E.D., Van Hekken D.L., Holsinger V.H. Effect of sodium chloride on the solubility of caseins. J. Dairy Sci. 1994, 77:1216-1222.
    • (1994) J. Dairy Sci. , vol.77 , pp. 1216-1222
    • Strange, E.D.1    Van Hekken, D.L.2    Holsinger, V.H.3
  • 74
    • 33751222558 scopus 로고    scopus 로고
    • Solvent-mediated disruption of bovine casein micelles at alkaline pH
    • Vaia B., Smiddy M.A., Kelly A.L., Huppertz T. Solvent-mediated disruption of bovine casein micelles at alkaline pH. J. Agric. Food Chem. 2006, 54:8288-8293.
    • (2006) J. Agric. Food Chem. , vol.54 , pp. 8288-8293
    • Vaia, B.1    Smiddy, M.A.2    Kelly, A.L.3    Huppertz, T.4
  • 75
    • 85025797643 scopus 로고
    • On the stability of casein micelles
    • Walstra P. On the stability of casein micelles. J. Dairy Sci. 1990, 73:1965-1979.
    • (1990) J. Dairy Sci. , vol.73 , pp. 1965-1979
    • Walstra, P.1
  • 77
    • 0030203536 scopus 로고    scopus 로고
    • A method for isolating β-casein
    • Ward L.S., Bastian E.D. A method for isolating β-casein. J. Dairy Sci. 1996, 79:1332-1339.
    • (1996) J. Dairy Sci. , vol.79 , pp. 1332-1339
    • Ward, L.S.1    Bastian, E.D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.