메뉴 건너뛰기




Volumn 99, Issue 2, 2016, Pages 1083-1094

Effect of adjusted pH prior to ultrafiltration of skim milk on membrane performance and physical functionality of milk protein concentrate

Author keywords

Calcium; Milk protein concentrate; PH; Ultrafiltration

Indexed keywords

ARTIFICIAL MEMBRANE; CASEIN; MICELLE; MILK PROTEIN; POWDER;

EID: 84955662598     PISSN: 00220302     EISSN: 15253198     Source Type: Journal    
DOI: 10.3168/jds.2015-9842     Document Type: Article
Times cited : (32)

References (66)
  • 1
    • 0000011321 scopus 로고    scopus 로고
    • Heat-induced, pH-dependent dissociation of casein micelles on heating reconstituted skim milk at temperature below 100°C
    • Anema S.G., Klostermeyer H. Heat-induced, pH-dependent dissociation of casein micelles on heating reconstituted skim milk at temperature below 100°C. J. Agric. Food Chem. 1997, 45:1108-1115.
    • (1997) J. Agric. Food Chem. , vol.45 , pp. 1108-1115
    • Anema, S.G.1    Klostermeyer, H.2
  • 3
    • 0000299524 scopus 로고
    • Determination of interfacial area in emulsions using turbidimetric and droplet size data: Correction of the formula for emulsifying activity index
    • Cameron D.R., Weber M.E., Idziak E.S., Neufeld R.J., Cooper D.G. Determination of interfacial area in emulsions using turbidimetric and droplet size data: Correction of the formula for emulsifying activity index. J. Agric. Food Chem. 1991, 39:655-659.
    • (1991) J. Agric. Food Chem. , vol.39 , pp. 655-659
    • Cameron, D.R.1    Weber, M.E.2    Idziak, E.S.3    Neufeld, R.J.4    Cooper, D.G.5
  • 4
    • 77951667418 scopus 로고    scopus 로고
    • Secondary structure of food proteins by Fourier transform spectroscopy in the mid-infrared region
    • Carbonaro M., Nucara A. Secondary structure of food proteins by Fourier transform spectroscopy in the mid-infrared region. Amino Acids 2010, 38:679-690.
    • (2010) Amino Acids , vol.38 , pp. 679-690
    • Carbonaro, M.1    Nucara, A.2
  • 5
    • 32244441097 scopus 로고    scopus 로고
    • Food emulsions-Their structures and structure-forming properties
    • Dalgleish D.G. Food emulsions-Their structures and structure-forming properties. Food Hydrocoll. 2006, 20:415-422.
    • (2006) Food Hydrocoll. , vol.20 , pp. 415-422
    • Dalgleish, D.G.1
  • 6
    • 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
  • 7
    • 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
  • 9
    • 0000298096 scopus 로고    scopus 로고
    • Properties of emulsions stabilized with milk proteins: Overview of some recent developments
    • Dickinson E. Properties of emulsions stabilized with milk proteins: Overview of some recent developments. J. Dairy Sci. 1997, 80:2607-2619.
    • (1997) J. Dairy Sci. , vol.80 , pp. 2607-2619
    • Dickinson, E.1
  • 10
    • 21444460240 scopus 로고    scopus 로고
    • Depletion flocculation of emulsions containing unadsorbed sodium caseinate
    • Dickinson E., Golding M. Depletion flocculation of emulsions containing unadsorbed sodium caseinate. Food Hydrocoll. 1997, 11:13-18.
    • (1997) Food Hydrocoll. , vol.11 , pp. 13-18
    • Dickinson, E.1    Golding, M.2
  • 11
    • 70350292443 scopus 로고    scopus 로고
    • Regression models for density and viscosity of ultrafiltration milk concentrates
    • Dinkov K., Dushkova M., Toshkov N. Regression models for density and viscosity of ultrafiltration milk concentrates. Bulg. J. Agric. Sci. 2008, 14:542-548.
    • (2008) Bulg. J. Agric. Sci. , vol.14 , pp. 542-548
    • Dinkov, K.1    Dushkova, M.2    Toshkov, N.3
  • 12
    • 84858990585 scopus 로고    scopus 로고
    • Functional properties of whey proteins microparticulated at low pH
    • Dissanayake M., Liyanaarachchi S., Vasiljevic T. Functional properties of whey proteins microparticulated at low pH. J. Dairy Sci. 2012, 95:1667-1679.
    • (2012) J. Dairy Sci. , vol.95 , pp. 1667-1679
    • Dissanayake, M.1    Liyanaarachchi, S.2    Vasiljevic, T.3
  • 13
    • 33745609556 scopus 로고    scopus 로고
    • Enzymatic cross-linking of β-lactoglobulin: Conformational properties using FTIR spectroscopy
    • Eissa A.S., Puhl C., Kadla J.F., Khan S.A. Enzymatic cross-linking of β-lactoglobulin: Conformational properties using FTIR spectroscopy. Biomacromolecules 2006, 7:1707-1713.
    • (2006) Biomacromolecules , vol.7 , pp. 1707-1713
    • Eissa, A.S.1    Puhl, C.2    Kadla, J.F.3    Khan, S.A.4
  • 14
    • 79953685887 scopus 로고    scopus 로고
    • Milk reversibility following reduction and restoration of pH
    • Ezeh V.N., Lewis M.J. Milk reversibility following reduction and restoration of pH. Int. J. Dairy Technol. 2011, 64:179-187.
    • (2011) Int. J. Dairy Technol. , vol.64 , pp. 179-187
    • Ezeh, V.N.1    Lewis, M.J.2
  • 15
    • 0030295616 scopus 로고    scopus 로고
    • Microstructure of oil-in-water low-fat emulsions containing skim milk powder and locust bean gum
    • Ferragut V., Chiralt A. Microstructure of oil-in-water low-fat emulsions containing skim milk powder and locust bean gum. Food Sci. Technol. (Campinas.) 1996, 29:648-653.
    • (1996) Food Sci. Technol. (Campinas.) , vol.29 , pp. 648-653
    • Ferragut, V.1    Chiralt, A.2
  • 17
    • 23744517126 scopus 로고    scopus 로고
    • The minerals of milk
    • Gaucheron F. The minerals of milk. Reprod. Nutr. Dev. 2005, 45:473-483.
    • (2005) Reprod. Nutr. Dev. , vol.45 , pp. 473-483
    • Gaucheron, F.1
  • 18
    • 0342599626 scopus 로고
    • The relation between the heat stability of milk and its chemical composition
    • Ghatak P.K., Bandyopadyay A.K., Gupta M.P. The relation between the heat stability of milk and its chemical composition. J. Dairy Res. 1989, 8:165-168.
    • (1989) J. Dairy Res. , vol.8 , pp. 165-168
    • Ghatak, P.K.1    Bandyopadyay, A.K.2    Gupta, M.P.3
  • 19
    • 0023881538 scopus 로고
    • The disaggregation of calcium-depleted casein micelles
    • Griffin M.C.A., Lyster R.L.J., Price J.C. The disaggregation of calcium-depleted casein micelles. Eur. J. Biochem. 1988, 174:339-343.
    • (1988) Eur. J. Biochem. , vol.174 , pp. 339-343
    • Griffin, M.C.A.1    Lyster, R.L.J.2    Price, J.C.3
  • 20
    • 0019363851 scopus 로고
    • Protein stabilized foams and emulsions
    • Halling P.J. Protein stabilized foams and emulsions. Crit. Rev. Food Sci. Nutr. 1981, 15:155-203.
    • (1981) Crit. Rev. Food Sci. Nutr. , vol.15 , pp. 155-203
    • Halling, P.J.1
  • 21
    • 77954546506 scopus 로고    scopus 로고
    • Protein conformational modifications and kinetics of water-protein interactions in milk protein concentrate powder upon aging: Effect on solubility
    • Haque E., Bhandari B.R., Gidley M.J., Deeth H.C., Møller S.M., Whittaker A.K. Protein conformational modifications and kinetics of water-protein interactions in milk protein concentrate powder upon aging: Effect on solubility. J. Agric. Food Chem. 2010, 58:7748-7755.
    • (2010) J. Agric. Food Chem. , vol.58 , pp. 7748-7755
    • Haque, E.1    Bhandari, B.R.2    Gidley, M.J.3    Deeth, H.C.4    Møller, S.M.5    Whittaker, A.K.6
  • 22
    • 84877917681 scopus 로고    scopus 로고
    • Fouling of dairy components on hydrophobic polytetrafluoroethylene (PTFE) membranes for membrane distillation
    • Hausmann A., Sanciolo P., Vasiljevic T., Weeks M., Schroën K., Gray S., Duke M. Fouling of dairy components on hydrophobic polytetrafluoroethylene (PTFE) membranes for membrane distillation. J. Membr. Sci. 2013, 442:149-159.
    • (2013) J. Membr. Sci. , vol.442 , pp. 149-159
    • Hausmann, A.1    Sanciolo, P.2    Vasiljevic, T.3    Weeks, M.4    Schroën, K.5    Gray, S.6    Duke, M.7
  • 23
    • 30744444212 scopus 로고    scopus 로고
    • Protein interactions in milk protein concentrate powders
    • Havea P. Protein interactions in milk protein concentrate powders. Int. Dairy J. 2006, 16:415-422.
    • (2006) Int. Dairy J. , vol.16 , pp. 415-422
    • Havea, P.1
  • 24
    • 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
  • 25
    • 0003134635 scopus 로고
    • Effect of heating and cooling on the milk salts and their interaction with casein
    • IDF special issue 9501, International Dairy Federation, Brussels, Belgium, P.F. Fox (Ed.)
    • Holt C. Effect of heating and cooling on the milk salts and their interaction with casein. Heat Induced Changes in Milk 1995, 105-133. IDF special issue 9501, International Dairy Federation, Brussels, Belgium. P.F. Fox (Ed.).
    • (1995) Heat Induced Changes in Milk , pp. 105-133
    • Holt, C.1
  • 26
    • 0001031111 scopus 로고
    • Effect of colloidal calcium phosphate content and free calcium ion concentration in milk serum on the dissociation of bovine casein micelles
    • Holt C., Davies D.T., Law A.J.R. Effect of colloidal calcium phosphate content and free calcium ion concentration in milk serum on the dissociation of bovine casein micelles. J. Dairy Res. 1986, 53:557-572.
    • (1986) J. Dairy Res. , vol.53 , pp. 557-572
    • Holt, C.1    Davies, D.T.2    Law, A.J.R.3
  • 27
    • 80051718073 scopus 로고    scopus 로고
    • Influence of mixtures of calcium-chelating salt on the physicochemical properties of casein micelles
    • Kaliappan S., Lucey J.A. Influence of mixtures of calcium-chelating salt on the physicochemical properties of casein micelles. J. Dairy Sci. 2011, 94:4255-4263.
    • (2011) J. Dairy Sci. , vol.94 , pp. 4255-4263
    • Kaliappan, S.1    Lucey, J.A.2
  • 29
    • 34548094323 scopus 로고    scopus 로고
    • Fourier transform infrared spectroscopic analysis of protein secondary structures
    • Kong J., Yu S. Fourier transform infrared spectroscopic analysis of protein secondary structures. Acta Biochim. Biophys. Sin. (Shanghai) 2007, 39:549-559.
    • (2007) Acta Biochim. Biophys. Sin. (Shanghai) , vol.39 , pp. 549-559
    • Kong, J.1    Yu, S.2
  • 30
    • 0000702316 scopus 로고    scopus 로고
    • Effects of acidification and storage of milk on dissociation of bovine casein micelles
    • Law A.J.R., Leaver J.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.J.2
  • 31
    • 0035178503 scopus 로고    scopus 로고
    • Molecular structure and interaction of biopolymers as viewed by Fourier transform infrared spectroscopy: Model studies on β-lactoglobulin
    • Lefevre T., Subirade M. Molecular structure and interaction of biopolymers as viewed by Fourier transform infrared spectroscopy: Model studies on β-lactoglobulin. Food Hydrocoll. 2001, 15:365-376.
    • (2001) Food Hydrocoll. , vol.15 , pp. 365-376
    • Lefevre, T.1    Subirade, M.2
  • 32
    • 78751614647 scopus 로고    scopus 로고
    • The measurement and significance of ionic calcium in milk. A review
    • Lewis M.J. The measurement and significance of ionic calcium in milk. A review. Int. J. Dairy Technol. 2011, 64:1-13.
    • (2011) Int. J. Dairy Technol. , vol.64 , pp. 1-13
    • Lewis, M.J.1
  • 33
    • 84923317052 scopus 로고    scopus 로고
    • Calcium release from milk concentrated by ultrafiltration and diafiltration
    • Li Y., Corredig M. Calcium release from milk concentrated by ultrafiltration and diafiltration. J. Dairy Sci. 2014, 97:5294-5302.
    • (2014) J. Dairy Sci. , vol.97 , pp. 5294-5302
    • Li, Y.1    Corredig, M.2
  • 34
    • 46049093569 scopus 로고    scopus 로고
    • PH-Dependent structures and properties of 690 casein micelles
    • Liu Y., Guo R. pH-Dependent structures and properties of 690 casein micelles. Biophys. Chem. 2008, 136:67-73.
    • (2008) Biophys. Chem. , vol.136 , pp. 67-73
    • Liu, Y.1    Guo, R.2
  • 35
    • 84922368364 scopus 로고    scopus 로고
    • Controlling heat induced aggregation of whey proteins by casein inclusion in concentrated protein dispersions
    • Liyanaarachchi W.S., Ramchandran L., Vasiljevic T. Controlling heat induced aggregation of whey proteins by casein inclusion in concentrated protein dispersions. Int. Dairy J. 2015, 44:21-30.
    • (2015) Int. Dairy J. , vol.44 , pp. 21-30
    • Liyanaarachchi, W.S.1    Ramchandran, L.2    Vasiljevic, T.3
  • 36
    • 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
  • 37
    • 84921907029 scopus 로고    scopus 로고
    • Lower ultrafiltration temperature improves membrane performance and emulsifying properties of milk protein concentrates
    • Luo X., Ramchandran L., Vasiljevic T. Lower ultrafiltration temperature improves membrane performance and emulsifying properties of milk protein concentrates. Dairy Sci. Technol. 2015, 95:15-31.
    • (2015) Dairy Sci. Technol. , vol.95 , pp. 15-31
    • Luo, X.1    Ramchandran, L.2    Vasiljevic, T.3
  • 38
    • 33947171472 scopus 로고    scopus 로고
    • Acid-induced gelation of milk protein concentrates with added pectin: Effect of casein micelle dissociation
    • Matia-Merino L., Singh H. Acid-induced gelation of milk protein concentrates with added pectin: Effect of casein micelle dissociation. Food Hydrocoll. 2007, 21:765-775.
    • (2007) Food Hydrocoll. , vol.21 , pp. 765-775
    • Matia-Merino, L.1    Singh, H.2
  • 40
    • 84948978013 scopus 로고    scopus 로고
    • Casein micelle structure, functions, and interactions
    • Springer, New York, NY, P.F. Fox, P.L.H. McSweeney (Eds.)
    • McMahon D.J., Oommen B.S. Casein micelle structure, functions, and interactions. Advanced Dairy Chemistry: Proteins 2013, 185-211. Springer, New York, NY. 4th. P.F. Fox, P.L.H. McSweeney (Eds.).
    • (2013) Advanced Dairy Chemistry: Proteins , pp. 185-211
    • McMahon, D.J.1    Oommen, B.S.2
  • 41
    • 69749112857 scopus 로고    scopus 로고
    • Impaired or accelerated aggregation of proteins in sterilised milk by adding surfactants
    • Mellema M., de Groot P.W.N., Golding M. Impaired or accelerated aggregation of proteins in sterilised milk by adding surfactants. Int. Dairy J. 2009, 19:728-736.
    • (2009) Int. Dairy J. , vol.19 , pp. 728-736
    • Mellema, M.1    de Groot, P.W.N.2    Golding, M.3
  • 43
    • 85005747544 scopus 로고
    • Optimization of the heat stability of protein-rich concentrates prepared by ultrafiltration of skim-milk
    • Muir D.D., Sweetsur A.W.M. Optimization of the heat stability of protein-rich concentrates prepared by ultrafiltration of skim-milk. J. Food Technol. 1984, 19:263-271.
    • (1984) J. Food Technol. , vol.19 , pp. 263-271
    • Muir, D.D.1    Sweetsur, A.W.M.2
  • 44
    • 84875041239 scopus 로고    scopus 로고
    • Colloidal properties of concentrated heated milk
    • Nair P.K., Dalgleish D.G., Corredig M. Colloidal properties of concentrated heated milk. Soft Matter 2013, 9:3815-3824.
    • (2013) Soft Matter , vol.9 , pp. 3815-3824
    • Nair, P.K.1    Dalgleish, D.G.2    Corredig, M.3
  • 45
    • 0742331980 scopus 로고    scopus 로고
    • Heat induced coagulation of milk
    • Kluwer Academic/Plenum Publishers, New York, NY, P.F. Fox, P.L.H. McSweeney (Eds.)
    • O'Connell J.E., Fox P.F. Heat induced coagulation of milk. Advanced Dairy Chemistry 2003, 887-930. Kluwer Academic/Plenum Publishers, New York, NY. P.F. Fox, P.L.H. McSweeney (Eds.).
    • (2003) Advanced Dairy Chemistry , pp. 887-930
    • O'Connell, J.E.1    Fox, P.F.2
  • 46
    • 2142851047 scopus 로고
    • Fouling of hollow fibre membranes during ultrafiltration of skim miIk
    • Patel R.S., Reuter H. Fouling of hollow fibre membranes during ultrafiltration of skim miIk. Milchwissenschaft 1985, 40:731-733.
    • (1985) Milchwissenschaft , vol.40 , pp. 731-733
    • Patel, R.S.1    Reuter, H.2
  • 47
    • 33947092713 scopus 로고
    • Emulsifying properties of proteins. Evaluation of a turbidimetric technique
    • Pearce K.N., Kinsella J.E. Emulsifying properties of proteins. Evaluation of a turbidimetric technique. J. Agric. Food Chem. 1978, 26:716-723.
    • (1978) J. Agric. Food Chem. , vol.26 , pp. 716-723
    • Pearce, K.N.1    Kinsella, J.E.2
  • 48
    • 84971929326 scopus 로고
    • Mineral and protein equillibria between the colloidal and soluble phase of milk at low temperature
    • Pierre A., Brule G. Mineral and protein equillibria between the colloidal and soluble phase of milk at low temperature. J. Dairy Res. 1981, 48:417-428.
    • (1981) J. Dairy Res. , vol.48 , pp. 417-428
    • Pierre, A.1    Brule, G.2
  • 49
    • 0002295609 scopus 로고
    • Observations on the seaonal variations in the salt balance of concentrated milk
    • Pouliot Y., Boulet M. Observations on the seaonal variations in the salt balance of concentrated milk. Int. Dairy J. 1995, 5:75-85.
    • (1995) Int. Dairy J. , vol.5 , pp. 75-85
    • Pouliot, Y.1    Boulet, M.2
  • 51
  • 52
    • 0033058274 scopus 로고    scopus 로고
    • Direct sedimentation analysis of interference optical data in analytical ultracentrifugation
    • Schuck P., Demeler B. Direct sedimentation analysis of interference optical data in analytical ultracentrifugation. Biophys. J. 1999, 76:2288-2296.
    • (1999) Biophys. J. , vol.76 , pp. 2288-2296
    • Schuck, P.1    Demeler, B.2
  • 53
    • 0036154258 scopus 로고    scopus 로고
    • Size-distribution analysis of proteins by analytical ultracentrifugation: Strategies and application to model systems
    • Schuck P., Perugini M.A., Gonzales N.R., Howlett G.J., Schubert D. Size-distribution analysis of proteins by analytical ultracentrifugation: Strategies and application to model systems. Biophys. J. 2002, 82:1096-1111.
    • (2002) Biophys. J. , vol.82 , pp. 1096-1111
    • Schuck, P.1    Perugini, M.A.2    Gonzales, N.R.3    Howlett, G.J.4    Schubert, D.5
  • 54
    • 84874438660 scopus 로고    scopus 로고
    • PH-induced demineralization of casein micelles modifies their physico-chemical and foaming properties
    • Silva N.N., Piot M., de Carvalho A.F., Violleau F., Fameau A.-L., Gaucheron F. pH-induced demineralization of casein micelles modifies their physico-chemical and foaming properties. Food Hydrocoll. 2013, 32:322-330.
    • (2013) Food Hydrocoll. , vol.32 , pp. 322-330
    • Silva, N.N.1    Piot, M.2    de Carvalho, A.F.3    Violleau, F.4    Fameau, A.-L.5    Gaucheron, F.6
  • 55
    • 0039036625 scopus 로고
    • Effect of ultrafiltration of skim milk on casein micelle size distrbution in retentate
    • Srilaorkul S., Ozimek L., Ooraikul B., Hadziyev D., Wolfe F. Effect of ultrafiltration of skim milk on casein micelle size distrbution in retentate. J. Dairy Sci. 1991, 74:50-57.
    • (1991) J. Dairy Sci. , vol.74 , pp. 50-57
    • Srilaorkul, S.1    Ozimek, L.2    Ooraikul, B.3    Hadziyev, D.4    Wolfe, F.5
  • 56
    • 0001232824 scopus 로고
    • Combined effect of temperature, acidification and diafiltration on composition of skim milk retentate and permeate
    • St-Gelais D., Hache S., Gros-Louis M. Combined effect of temperature, acidification and diafiltration on composition of skim milk retentate and permeate. J. Dairy Sci. 1992, 75:1167-1172.
    • (1992) J. Dairy Sci. , vol.75 , pp. 1167-1172
    • St-Gelais, D.1    Hache, S.2    Gros-Louis, M.3
  • 57
    • 0011339018 scopus 로고
    • The use of permitted additives and heat-treatment to optimize the heat-stability of skim milk and concentrated skim milk
    • Sweetsur A.W.M., Muir D.D. The use of permitted additives and heat-treatment to optimize the heat-stability of skim milk and concentrated skim milk. J. Soc. Dairy Technol. 1980, 33:10-11.
    • (1980) J. Soc. Dairy Technol. , vol.33 , pp. 10-11
    • Sweetsur, A.W.M.1    Muir, D.D.2
  • 58
    • 0033826654 scopus 로고    scopus 로고
    • Mineral and casein equilibrium in milk: Effects of added salts and calcium-chelating agents
    • Udabage P., McKinnon I.R., Augustin M.A. Mineral and casein equilibrium in milk: Effects of added salts and calcium-chelating agents. J. Dairy Res. 2000, 67:361-370.
    • (2000) J. Dairy Res. , vol.67 , pp. 361-370
    • Udabage, P.1    McKinnon, I.R.2    Augustin, M.A.3
  • 59
    • 84858784796 scopus 로고    scopus 로고
    • Modified water solubility of milk protein concentrate powders through the application of static high pressure treatment
    • Udabage P., Puvanenthiran A., Yoo J.A., Versteeg C., Augustin M.A. Modified water solubility of milk protein concentrate powders through the application of static high pressure treatment. J. Dairy Res. 2012, 79:76-83.
    • (2012) J. Dairy Res. , vol.79 , pp. 76-83
    • Udabage, P.1    Puvanenthiran, A.2    Yoo, J.A.3    Versteeg, C.4    Augustin, M.A.5
  • 60
    • 0001558145 scopus 로고
    • PH-induced physico-chemical changes of casein micelles in milk and their effect on renneting. 1. Effects of acidification on physico-chemical properties
    • Van Hooydonk A.C.M., Hagedoorn H.G., Boerrigter I.J. pH-induced physico-chemical changes of casein micelles in milk and their effect on renneting. 1. Effects of acidification on physico-chemical 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    Hagedoorn, H.G.2    Boerrigter, I.J.3
  • 61
    • 0043241649 scopus 로고    scopus 로고
    • Casein-whey protein interactions in heated milk: The influence of pH
    • Vasbinder A.J., de Kruif C.G. Casein-whey protein interactions in heated milk: The influence of pH. Int. Dairy J. 2003, 13:669-677.
    • (2003) Int. Dairy J. , vol.13 , pp. 669-677
    • Vasbinder, A.J.1    de Kruif, C.G.2
  • 62
    • 0033430794 scopus 로고    scopus 로고
    • Temperature effect on behavior of minerals during ultrafiltration of skim milk and acid whey
    • Vasiljevic T., Jelen P. Temperature effect on behavior of minerals during ultrafiltration of skim milk and acid whey. Milchwissenschaft 1999, 54:243-246.
    • (1999) Milchwissenschaft , vol.54 , pp. 243-246
    • Vasiljevic, T.1    Jelen, P.2
  • 63
    • 84974078328 scopus 로고
    • The structure of casein micelles between pH 5-5 and 6 7 as determined by light-scattering, electron microscopy and voluminosity experiments
    • Vreeman H.J., Van Markwijk B.W., Both P. The structure of casein micelles between pH 5-5 and 6 7 as determined by light-scattering, electron microscopy and voluminosity experiments. J. Dairy Res. 1989, 56:463-470.
    • (1989) J. Dairy Res. , vol.56 , pp. 463-470
    • Vreeman, H.J.1    Van Markwijk, B.W.2    Both, P.3
  • 64
    • 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
  • 65
    • 41849088866 scopus 로고    scopus 로고
    • Role of protein aggregation in heat-induced heat stability during milk powder manufacture
    • Williams R.P.W., D'ath L., Zisu B. Role of protein aggregation in heat-induced heat stability during milk powder manufacture. Dairy Sci. Technol. 2008, 88:121-147.
    • (2008) Dairy Sci. Technol. , vol.88 , pp. 121-147
    • Williams, R.P.W.1    D'ath, L.2    Zisu, B.3
  • 66
    • 78049267149 scopus 로고    scopus 로고
    • Functional properties of milk protein concentrates: Emulsifying properties, adsorption and stability of emulsions
    • Ye A. Functional properties of milk protein concentrates: Emulsifying properties, adsorption and stability of emulsions. Int. Dairy J. 2011, 21:14-20.
    • (2011) Int. Dairy J. , vol.21 , pp. 14-20
    • Ye, A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.