메뉴 건너뛰기




Volumn 61, Issue 38, 2013, Pages 9260-9268

Improving clarity and stability of skim milk powder dispersions by dissociation of casein micelles at pH 11.0 and acidification with citric acid

Author keywords

alkaline dissociation; casein micelles; citric acid; dispersibility; nanoscale structure; skim milk powder

Indexed keywords

ACIDIC CONDITIONS; CASEIN MICELLES; CHELATING EFFECT; DISPERSIBILITIES; NANOSCALE STRUCTURE; NEGATIVE ZETA POTENTIALS; NOVEL APPLICATIONS; SKIM MILK POWDER;

EID: 84884848988     PISSN: 00218561     EISSN: 15205118     Source Type: Journal    
DOI: 10.1021/jf402870y     Document Type: Article
Times cited : (44)

References (41)
  • 1
    • 27144501029 scopus 로고    scopus 로고
    • Milk proteins: General and historical aspects
    • 3 rd ed. Fox, P. F. Elsevier: New York, NY, Vol. - 41
    • Fox, P. F. Milk proteins: general and historical aspects. In Advanced dairy chemistry: proteins, 3 rd ed.; Fox, P. F., Ed.; Elsevier: New York, NY, 2003; Vol. 1, pp 1-41.
    • (2003) Advanced Dairy Chemistry: Proteins , vol.1 , pp. 1
    • Fox, P.F.1
  • 2
    • 0242571815 scopus 로고    scopus 로고
    • The use of sedimentation field flow fractionation and photon correlation spectroscopy in the characterization of casein micelles
    • Udabage, P.; McKinnon, I. R.; Augustin, M. A. The use of sedimentation field flow fractionation and photon correlation spectroscopy in the characterization of casein micelles J. Dairy Res. 2003, 70, 453-459
    • (2003) J. Dairy Res. , vol.70 , pp. 453-459
    • Udabage, P.1    McKinnon, I.R.2    Augustin, M.A.3
  • 3
    • 44549088735 scopus 로고    scopus 로고
    • The casein micelle: Historical aspects, current concepts and significance
    • Fox, P. F.; Brodkorb, A. The casein micelle: historical aspects, current concepts and significance Int. Dairy J. 2008, 18, 677-684
    • (2008) Int. Dairy J. , vol.18 , pp. 677-684
    • Fox, P.F.1    Brodkorb, A.2
  • 4
    • 0033826654 scopus 로고    scopus 로고
    • Mineral and casein equilibria in milk: Effects of added salts and calcium-chelating agents
    • Udabage, P.; McKinnon, I. R.; Augustin, M. A. Mineral and casein equilibria 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
  • 5
    • 0000109049 scopus 로고
    • κ-Casein and the Stabilization of Casein Micelles
    • Waugh, D. F.; von Hippel, P. H. κ-Casein and the Stabilization of Casein Micelles J. Am. Chem. Soc. 1956, 78, 4576-4582
    • (1956) J. Am. Chem. Soc. , vol.78 , pp. 4576-4582
    • Waugh, D.F.1    Von Hippel, P.H.2
  • 6
    • 0022862357 scopus 로고
    • Electrophoretic and hydrodynamic properties of bovine casein micelles interpreted in terms of particles with an outer hairy layer
    • Holt, C.; Dalgleish, D. G. Electrophoretic and hydrodynamic properties of bovine casein micelles interpreted in terms of particles with an outer hairy layer J. Colloid Interface Sci. 1986, 114, 513-524
    • (1986) J. Colloid Interface Sci. , vol.114 , pp. 513-524
    • Holt, C.1    Dalgleish, D.G.2
  • 7
    • 0037101011 scopus 로고    scopus 로고
    • Stability of casein micelles in milk
    • Tuinier, R.; De Kruif, C. Stability of casein micelles in milk J. Chem. Phys. 2002, 117, 1290-1295
    • (2002) J. Chem. Phys. , vol.117 , pp. 1290-1295
    • Tuinier, R.1    De Kruif, C.2
  • 8
    • 0000561389 scopus 로고    scopus 로고
    • Casein micelles as colloids: Surface structures and stabilities
    • Dalgleish, D. G. Casein micelles as colloids: surface structures and stabilities J. Dairy Sci. 1998, 81, 3013-3018
    • (1998) J. Dairy Sci. , vol.81 , pp. 3013-3018
    • Dalgleish, D.G.1
  • 9
    • 33947182943 scopus 로고    scopus 로고
    • Casein micelle as a natural nano-capsular vehicle for nutraceuticals
    • Semo, E.; Kesselman, E.; Danino, D.; Livney, Y. D. Casein micelle as a natural nano-capsular vehicle for nutraceuticals Food Hydrocolloids 2007, 21, 936-942
    • (2007) Food Hydrocolloids , vol.21 , pp. 936-942
    • Semo, E.1    Kesselman, E.2    Danino, D.3    Livney, Y.D.4
  • 10
    • 0030097895 scopus 로고    scopus 로고
    • Microencapsulation of volatiles by spray-drying in whey protein-based wall systems
    • Rosenberg, M.; Sheu, T. Microencapsulation of volatiles by spray-drying in whey protein-based wall systems Int. Dairy J. 1996, 6, 273-284
    • (1996) Int. Dairy J. , vol.6 , pp. 273-284
    • Rosenberg, M.1    Sheu, T.2
  • 11
    • 34249039632 scopus 로고    scopus 로고
    • Use of whey proteins for encapsulation and controlled delivery applications
    • Gunasekaran, S.; Ko, S.; Xiao, L. Use of whey proteins for encapsulation and controlled delivery applications J. Food Eng. 2007, 83, 31-40
    • (2007) J. Food Eng. , vol.83 , pp. 31-40
    • Gunasekaran, S.1    Ko, S.2    Xiao, L.3
  • 13
    • 33748435922 scopus 로고    scopus 로고
    • Disruption and reassociation of casein micelles under high pressure: Influence of milk serum composition and casein micelle concentration
    • Huppertz, T.; de Kruif, C. G. Disruption and reassociation of casein micelles under high pressure: influence of milk serum composition and casein micelle concentration J. Agric. Food. Chem. 2006, 54, 5903-5909
    • (2006) J. Agric. Food. Chem. , vol.54 , pp. 5903-5909
    • Huppertz, T.1    De Kruif, C.G.2
  • 14
    • 2942752365 scopus 로고    scopus 로고
    • Dissociation of caseins in high pressure-treated bovine milk
    • Huppertz, T.; Fox, P. F.; Kelly, A. L. Dissociation of caseins in high pressure-treated bovine milk Int. Dairy J. 2004, 14, 675-680
    • (2004) Int. Dairy J. , vol.14 , pp. 675-680
    • Huppertz, T.1    Fox, P.F.2    Kelly, A.L.3
  • 15
    • 77749323470 scopus 로고    scopus 로고
    • Casein micelle dissociation in skim milk during high-pressure treatment: Effects of pressure, pH, and temperature
    • Orlien, V.; Boserup, L.; Olsen, K. Casein micelle dissociation in skim milk during high-pressure treatment: effects of pressure, pH, and temperature J. Dairy Sci. 2010, 93, 12-18
    • (2010) J. Dairy Sci. , vol.93 , pp. 12-18
    • Orlien, V.1    Boserup, L.2    Olsen, K.3
  • 16
    • 0016718784 scopus 로고
    • A discussion of pressure-volume effects in aqueous protein solutions
    • Hvidt, A. A discussion of pressure-volume effects in aqueous protein solutions J. Theor. Biol. 1975, 50, 245-252
    • (1975) J. Theor. Biol. , vol.50 , pp. 245-252
    • Hvidt, A.1
  • 17
    • 0034838014 scopus 로고    scopus 로고
    • Mechanism for the ethanol-dependent heat-induced dissociation of casein micelles
    • John, E. O. C.; Kelly, A. L.; Fox, P. F.; de Kruif, K. G. Mechanism for the ethanol-dependent heat-induced dissociation of casein micelles J. Agric. Food. Chem. 2001, 49, 4424-4428
    • (2001) J. Agric. Food. Chem. , vol.49 , pp. 4424-4428
    • John, E.O.C.1    Kelly, A.L.2    Fox, P.F.3    De Kruif, K.G.4
  • 19
    • 70749103845 scopus 로고    scopus 로고
    • Microstructural changes in casein supramolecules during acidification of skim milk
    • McMahon, D. J.; Du, H.; McManus, W.; Larsen, K. Microstructural changes in casein supramolecules during acidification of skim milk J. Dairy Sci. 2009, 92, 5854-5867
    • (2009) J. Dairy Sci. , vol.92 , pp. 5854-5867
    • McMahon, D.J.1    Du, H.2    McManus, W.3    Larsen, K.4
  • 20
    • 0042979741 scopus 로고    scopus 로고
    • Acid-induced dissociation of casein micelles in milk: Effects of heat treatment
    • Singh, H.; Roberts, M. S.; Munro, P. A.; Teo, C. T. Acid-induced dissociation of casein micelles in milk: Effects of heat treatment J. Dairy Sci. 1996, 79, 1340-1346
    • (1996) J. Dairy Sci. , vol.79 , pp. 1340-1346
    • Singh, H.1    Roberts, M.S.2    Munro, P.A.3    Teo, C.T.4
  • 21
    • 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
  • 22
    • 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
  • 23
    • 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
  • 24
    • 0015498925 scopus 로고
    • Effect of calcium ion on the structure of native bovine casein micelles
    • Lin, S. H.; Leong, S. L.; Dewan, R. K.; Bloomfield, V. A.; Morr, C. V. Effect of calcium ion on the structure of native bovine casein micelles Biochemistry 1972, 11, 1818-1821
    • (1972) Biochemistry , vol.11 , pp. 1818-1821
    • Lin, S.H.1    Leong, S.L.2    Dewan, R.K.3    Bloomfield, V.A.4    Morr, C.V.5
  • 25
    • 85010250153 scopus 로고
    • Complexing of Calcium by Hexametaphosphate, Oxalate, Citrate, and Edta in Milk. I. Effects of Complexing Agents on Turbidity and Rennet Coagulation1
    • Odagiri, S.; Nickerson, T. Complexing of Calcium by Hexametaphosphate, Oxalate, Citrate, and Edta in Milk. I. Effects of Complexing Agents on Turbidity and Rennet Coagulation1 J. Dairy Sci. 1964, 47, 1306-1309
    • (1964) J. Dairy Sci. , vol.47 , pp. 1306-1309
    • Odagiri, S.1    Nickerson, T.2
  • 26
    • 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
  • 27
    • 84866714768 scopus 로고    scopus 로고
    • Glycation of Whey Protein to Provide Steric Hindrance against Thermal Aggregation
    • Liu, G.; Zhong, Q. X. Glycation of Whey Protein To Provide Steric Hindrance against Thermal Aggregation J. Agric. Food Chem. 2012, 60, 9754-9762
    • (2012) J. Agric. Food Chem. , vol.60 , pp. 9754-9762
    • Liu, G.1    Zhong, Q.X.2
  • 28
    • 21844511439 scopus 로고
    • Analysis of major bovine-milk protein by online high-performanceliquid- chromatography and electrospray-ionization mass-spectrometry
    • Leonil, J.; Molle, D.; Gaucheron, F.; Arpino, P.; Guenot, P.; Maubois, J. L. Analysis of major bovine-milk protein by online high-performanceliquid- chromatography and electrospray-ionization mass-spectrometry Lait 1995, 75, 193-210
    • (1995) Lait , vol.75 , pp. 193-210
    • Leonil, J.1    Molle, D.2    Gaucheron, F.3    Arpino, P.4    Guenot, P.5    Maubois, J.L.6
  • 29
    • 0000197837 scopus 로고
    • Early indicators of chemical changes in foods due to enzymatic or non enzymatic browning reactions. I, Study on heat treated model systems
    • Lerici, C.; Barbanti, D.; Manzano, M.; Cherubin, S. Early indicators of chemical changes in foods due to enzymatic or non enzymatic browning reactions. I, Study on heat treated model systems Lebensm.-Wiss. Technol. 1990, 23, 289-294
    • (1990) Lebensm.-Wiss. Technol. , vol.23 , pp. 289-294
    • Lerici, C.1    Barbanti, D.2    Manzano, M.3    Cherubin, S.4
  • 30
    • 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
  • 33
    • 75149130837 scopus 로고    scopus 로고
    • Preparation of nanoparticles from denatured whey protein by pH-cycling treatment
    • Giroux, H. J.; Houde, J.; Britten, M. Preparation of nanoparticles from denatured whey protein by pH-cycling treatment Food Hydrocolloids 2010, 24, 341-346
    • (2010) Food Hydrocolloids , vol.24 , pp. 341-346
    • Giroux, H.J.1    Houde, J.2    Britten, M.3
  • 34
    • 0002935758 scopus 로고
    • Casein micelles
    • 1 st ed. Walstra, P. Jenness, R. John Wiley & Sons: Hoboken, NJ, Vol. - 253
    • Walstra, P.; Jenness, R. Casein micelles. In Dairy Chemistry and Physics, 1 st ed.; Walstra, P.; Jenness, R., Eds.; John Wiley & Sons: Hoboken, NJ, 1984; Vol. 1, pp 229-253.
    • (1984) Dairy Chemistry and Physics , vol.1 , pp. 229
    • Walstra, P.1    Jenness, R.2
  • 35
    • 0033807171 scopus 로고    scopus 로고
    • Rheological investigations of alkaline-induced gelation of skimmed milk and reconstituted skimmed milk concentrates
    • Hemar, Y.; Law, A. J. R.; Horne, D. S.; Leaver, J. Rheological investigations of alkaline-induced gelation of skimmed milk and reconstituted skimmed milk concentrates Food Hydrocolloids 2000, 14, 197-201
    • (2000) Food Hydrocolloids , vol.14 , pp. 197-201
    • Hemar, Y.1    Law, A.J.R.2    Horne, D.S.3    Leaver, J.4
  • 36
    • 0040551239 scopus 로고
    • Some effects of pyrophosphate and citrate ions upon the colloidal caseinate-phosphate micelles and ultrafiltrate of raw and heated skimmilk
    • Morr, C. Some effects of pyrophosphate and citrate ions upon the colloidal caseinate-phosphate micelles and ultrafiltrate of raw and heated skimmilk J. Dairy Sci. 1967, 50, 1038-1044
    • (1967) J. Dairy Sci. , vol.50 , pp. 1038-1044
    • Morr, C.1
  • 37
    • 0002429127 scopus 로고
    • Association of caseins and casein micelle structure
    • 1 st ed. Fox, P. F. Elsevier Applied Science: London, U.K. Vol. - 86
    • Schmidt, D. Association of caseins and casein micelle structure. In Developments in Dairy Chemistry, 1 st ed.; Fox, P. F., Ed.; Elsevier Applied Science: London, U.K., 1982; Vol. 1, pp 61-86.
    • (1982) Developments in Dairy Chemistry , vol.1 , pp. 61
    • Schmidt, D.1
  • 38
    • 70449501947 scopus 로고    scopus 로고
    • The Manufacture and Applications of Casein-Derived Ingredients
    • 1 st ed. Hui, Y. H. John Wiley & Sons: Hoboken, NJ, Vol. - 591
    • O'Connell, J. E.; Flynn, C. The Manufacture and Applications of Casein-Derived Ingredients. In Handbook of Food Products Manufacturing, 1 st ed.; Hui, Y. H., Ed.; John Wiley & Sons: Hoboken, NJ, 2007; Vol. 1, pp 557-591.
    • (2007) Handbook of Food Products Manufacturing , vol.1 , pp. 557
    • O'Connell, J.E.1    Flynn, C.2
  • 39
    • 84884888598 scopus 로고    scopus 로고
    • Aspects of thermoldynamics
    • 1 st ed. Walstra, P. Marcel Decker: New York, NY, Vol. - 60
    • Walstra, P. Aspects of thermoldynamics. In Physical Chemistry of Foods, 1 st ed.; Walstra, P., Ed.; Marcel Decker: New York, NY, 2002; Vol. 1, pp 55-60.
    • (2002) Physical Chemistry of Foods , vol.1 , pp. 55
    • Walstra, P.1
  • 41
    • 84982625768 scopus 로고
    • On the alkali treatment of proteins. III. Dephosphorylation of acid caseins and casein practions in an likaline medium
    • Freimuth, U.; Krause, W. On the alkali treatment of proteins. III. Dephosphorylation of acid caseins and casein practions in an likaline medium Nahrung 1980, 24, 317-326
    • (1980) Nahrung , vol.24 , pp. 317-326
    • Freimuth, U.1    Krause, W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.