메뉴 건너뛰기




Volumn 21, Issue 11, 2011, Pages 877-886

Reconstitution properties of micellar casein powder: Effects of composition and storage

Author keywords

[No Author keywords available]

Indexed keywords

CASEIN MICELLES; HIGHER ORDER; PROTEIN COMPOSITION; SHEET FORMATION; SMALL ANGLE X-RAY SCATTERING; SODIUM CASEINATE; STRUCTURAL CHANGE;

EID: 80051594043     PISSN: 09586946     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.idairyj.2011.05.004     Document Type: Article
Times cited : (82)

References (55)
  • 1
    • 34548034190 scopus 로고    scopus 로고
    • The challenge of drying method selection for protein pharmaceuticals: product quality implications
    • Abdul-Fattah A.M., Kalonia D.S., Pikal M.J. The challenge of drying method selection for protein pharmaceuticals: product quality implications. Journal of Pharmaceutical Sciences 2007, 96:1886-1916.
    • (2007) Journal of Pharmaceutical Sciences , vol.96 , pp. 1886-1916
    • Abdul-Fattah, A.M.1    Kalonia, D.S.2    Pikal, M.J.3
  • 2
    • 67651113623 scopus 로고    scopus 로고
    • Physico-chemical changes in casein micelles of buffalo and cow milks as a function of alkalinisation
    • Ahmad S., Piot M., Rousseau F., Grongnet J.F., Gaucheron F. Physico-chemical changes in casein micelles of buffalo and cow milks as a function of alkalinisation. Dairy Science and Technology 2009, 89:387-403.
    • (2009) Dairy Science and Technology , vol.89 , pp. 387-403
    • Ahmad, S.1    Piot, M.2    Rousseau, F.3    Grongnet, J.F.4    Gaucheron, F.5
  • 3
    • 25844444764 scopus 로고    scopus 로고
    • Effects of storage temperature on the solubility of milk protein concentrate
    • Anema S.G., Pinder D.N., Hunter R.J., Hemar Y. Effects of storage temperature on the solubility of milk protein concentrate. Food Hydrocolloids 2006, 20:386-393.
    • (2006) Food Hydrocolloids , vol.20 , pp. 386-393
    • Anema, S.G.1    Pinder, D.N.2    Hunter, R.J.3    Hemar, Y.4
  • 4
    • 77952708570 scopus 로고    scopus 로고
    • Insolubility of milk powder products - a mini review
    • Baldwin A.J. Insolubility of milk powder products - a mini review. Dairy Science and Technology 2010, 90:169-179.
    • (2010) Dairy Science and Technology , vol.90 , pp. 169-179
    • Baldwin, A.J.1
  • 5
    • 34848923747 scopus 로고    scopus 로고
    • Development of insolubility in dehydration of dairy milk powders
    • Baldwin A.J., Truong G.N.T. Development of insolubility in dehydration of dairy milk powders. Food and Bioproducts Processing 2007, 85:202-208.
    • (2007) Food and Bioproducts Processing , vol.85 , pp. 202-208
    • Baldwin, A.J.1    Truong, G.N.T.2
  • 6
    • 0011107453 scopus 로고
    • A neutron scattering study of the structure of a bimodal colloidal crystal
    • Bartlett P., Ottewill R.H. A neutron scattering study of the structure of a bimodal colloidal crystal. Journal of Chemical Physics 1992, 96:3306-3318.
    • (1992) Journal of Chemical Physics , vol.96 , pp. 3306-3318
    • Bartlett, P.1    Ottewill, R.H.2
  • 8
    • 80051587652 scopus 로고    scopus 로고
    • Milk protein products and processes. Patent WO01/41578.
    • Bhaskar, G. V., Singh, H., & Blazey, N. D. (2001). Milk protein products and processes. Patent WO01/41578.
    • (2001)
    • Bhaskar, G.V.1    Singh, H.2    Blazey, N.D.3
  • 9
    • 80051584210 scopus 로고    scopus 로고
    • Membrane filtered milk proteins varying in composition and functional attributes. Patent WO00/51440
    • Blazey, N. D., Knights, R. J., & Wu, C. (2000). Membrane filtered milk proteins varying in composition and functional attributes. Patent WO00/51440.
    • (2000)
    • Blazey, N.D.1    Knights, R.J.2    Wu, C.3
  • 10
    • 79955412568 scopus 로고
    • Apodization effects in Fourier transform infrared difference spectra
    • Bretzlaff R.S., Bahder T.B. Apodization effects in Fourier transform infrared difference spectra. Revue de Physique Appliquée 1986, 21:833-844.
    • (1986) Revue de Physique Appliquée , vol.21 , pp. 833-844
    • Bretzlaff, R.S.1    Bahder, T.B.2
  • 11
    • 0022691315 scopus 로고
    • Examination of the secondary structure of proteins by deconvolved FTIR spectra
    • Byler D.M., Susi H. Examination of the secondary structure of proteins by deconvolved FTIR spectra. Biopolymers 1986, 25:469-487.
    • (1986) Biopolymers , vol.25 , pp. 469-487
    • Byler, D.M.1    Susi, H.2
  • 12
    • 80051599284 scopus 로고    scopus 로고
    • Monovalent salt enhances solubility of milk protein concentrate. Patent WO02/096208.
    • Carr, A. J. (2002). Monovalent salt enhances solubility of milk protein concentrate. Patent WO02/096208.
    • (2002)
    • Carr, A.J.1
  • 13
    • 0031540994 scopus 로고    scopus 로고
    • A NMR relaxometry method for determining the reconstitutability and water-holding capacity of protein-rich milk powders
    • Davenel A., Schuck P., Marchal P. A NMR relaxometry method for determining the reconstitutability and water-holding capacity of protein-rich milk powders. Milchwissenschaft 1997, 52:35-39.
    • (1997) Milchwissenschaft , vol.52 , pp. 35-39
    • Davenel, A.1    Schuck, P.2    Marchal, P.3
  • 14
    • 0348114294 scopus 로고    scopus 로고
    • Casein micelle structure, functions and interactions
    • Kluwer Academic, New York, NY, USA, P.F. Fox, P.L.H. McSweeney (Eds.)
    • De Kruif C.G., Holt C. Casein micelle structure, functions and interactions. Advanced dairy chemistry - 1. Proteins 2003, 233-276. Kluwer Academic, New York, NY, USA. 3rd ed. P.F. Fox, P.L.H. McSweeney (Eds.).
    • (2003) Advanced dairy chemistry - 1. Proteins , pp. 233-276
    • De Kruif, C.G.1    Holt, C.2
  • 15
    • 19844370503 scopus 로고    scopus 로고
    • Enthalpy relaxation of bovine serum albumin and implications for its storage in the glassy state
    • Farahnaky A., Badii F., Farhat I.A., Mitchell J.R., Hill S.E. Enthalpy relaxation of bovine serum albumin and implications for its storage in the glassy state. Biopolymers 2005, 78:69-77.
    • (2005) Biopolymers , vol.78 , pp. 69-77
    • Farahnaky, A.1    Badii, F.2    Farhat, I.A.3    Mitchell, J.R.4    Hill, S.E.5
  • 16
    • 12344297731 scopus 로고    scopus 로고
    • Higher order structures of the caseins: a paradox?
    • Kluwer Academic, New York, NY, USA, P.F. Fox, P.L.H. McSweeney (Eds.)
    • Farrell H.M., Brown E.M., Hoagland P.D., Malin E.L. Higher order structures of the caseins: a paradox?. Advanced dairy chemistry - 1. Proteins 2003, 203-231. Kluwer Academic, New York, NY, USA. 3rd ed. P.F. Fox, P.L.H. McSweeney (Eds.).
    • (2003) Advanced dairy chemistry - 1. Proteins , pp. 203-231
    • Farrell, H.M.1    Brown, E.M.2    Hoagland, P.D.3    Malin, E.L.4
  • 17
    • 33748328257 scopus 로고    scopus 로고
    • The dissolution behaviour of native phosphocaseinate as a function of concentration and temperature using a rheological approach
    • Gaiani C., Scher J., Schuck P., Hardy J., Desobry S., Banon S. The dissolution behaviour of native phosphocaseinate as a function of concentration and temperature using a rheological approach. International Dairy Journal 2006, 16:1427-1434.
    • (2006) International Dairy Journal , vol.16 , pp. 1427-1434
    • Gaiani, C.1    Scher, J.2    Schuck, P.3    Hardy, J.4    Desobry, S.5    Banon, S.6
  • 18
    • 34247862268 scopus 로고    scopus 로고
    • Dairy powder rehydration: influence of protein state, incorporation mode, and agglomeration
    • Gaiani C., Schuck P., Scher J., Desobry S., Banon S. Dairy powder rehydration: influence of protein state, incorporation mode, and agglomeration. Journal of Dairy Science 2007, 90:570-581.
    • (2007) Journal of Dairy Science , vol.90 , pp. 570-581
    • Gaiani, C.1    Schuck, P.2    Scher, J.3    Desobry, S.4    Banon, S.5
  • 20
    • 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. Journal of Agricultural and Food Chemistry 2010, 58:7748-7755.
    • (2010) Journal of Agricultural and Food Chemistry , 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
  • 21
    • 30744444212 scopus 로고    scopus 로고
    • Protein interactions in milk protein concentrate powders
    • Havea P. Protein interactions in milk protein concentrate powders. International Dairy Journal 2006, 16:415-422.
    • (2006) International Dairy Journal , vol.16 , pp. 415-422
    • Havea, P.1
  • 22
    • 0001871181 scopus 로고    scopus 로고
    • The hairy casein micelle: evolution of the concept and its implications for dairy technology
    • Holt C., Horne D.S. The hairy casein micelle: evolution of the concept and its implications for dairy technology. Netherlands Milk and Dairy Journal 1996, 50:85-111.
    • (1996) Netherlands Milk and Dairy Journal , vol.50 , pp. 85-111
    • Holt, C.1    Horne, D.S.2
  • 24
    • 0029670230 scopus 로고    scopus 로고
    • Ability of β-casein phosphopeptide to modulate the precipitation of calcium phosphate by forming amorphous dicalcium phosphate nanoclusters
    • Holt C., Wahlgren M., Drakenberg T. Ability of β-casein phosphopeptide to modulate the precipitation of calcium phosphate by forming amorphous dicalcium phosphate nanoclusters. Biochemical Journal 1996, 314:1035-1039.
    • (1996) Biochemical Journal , vol.314 , pp. 1035-1039
    • Holt, C.1    Wahlgren, M.2    Drakenberg, T.3
  • 25
    • 77952683779 scopus 로고    scopus 로고
    • The influence of stirring speed, temperature and solid concentration on the rehydration time of micellar casein powder
    • Jeantet R., Schuck P., Six T., André C., Delaplace G. The influence of stirring speed, temperature and solid concentration on the rehydration time of micellar casein powder. Dairy Science and Technology 2010, 90:225-236.
    • (2010) Dairy Science and Technology , vol.90 , pp. 225-236
    • Jeantet, R.1    Schuck, P.2    Six, T.3    André, C.4    Delaplace, G.5
  • 27
    • 0030059491 scopus 로고    scopus 로고
    • Quantitation of the area of overlap between second-derivative amide I infrared spectra to determine the structural similarity of a protein in different states
    • Kendrick B.S., Dong A., Allison S.D., Manning M.C., Carpenter J.F. Quantitation of the area of overlap between second-derivative amide I infrared spectra to determine the structural similarity of a protein in different states. Journal of Pharmaceutical Sciences 1996, 85:155-158.
    • (1996) Journal of Pharmaceutical Sciences , vol.85 , pp. 155-158
    • Kendrick, B.S.1    Dong, A.2    Allison, S.D.3    Manning, M.C.4    Carpenter, J.F.5
  • 30
    • 33847718280 scopus 로고    scopus 로고
    • Effects of the environmental factors on the casein micelle structure studied by cryo transmission electron microscopy and small-angle X-ray scattering/ultrasmall-angle X-ray scattering
    • Marchin S., Putaux J.L., Pignon F., Léonil J. Effects of the environmental factors on the casein micelle structure studied by cryo transmission electron microscopy and small-angle X-ray scattering/ultrasmall-angle X-ray scattering. Journal of Chemical Physics 2007, 126:450101.
    • (2007) Journal of Chemical Physics , vol.126 , pp. 450101
    • Marchin, S.1    Putaux, J.L.2    Pignon, F.3    Léonil, J.4
  • 31
    • 80051596749 scopus 로고    scopus 로고
    • Effect of processing and storage on the reconstitution properties of whole milk and ultrafiltered skim milk powders. PhD. thesis, Massey University, Palmerston North, New Zealand
    • McKenna, A. B. (2000). Effect of processing and storage on the reconstitution properties of whole milk and ultrafiltered skim milk powders. PhD. thesis, Massey University, Palmerston North, New Zealand.
    • (2000)
    • McKenna, A.B.1
  • 32
    • 67349251542 scopus 로고    scopus 로고
    • Rehydration process of milk protein concentrate powder monitored by static light scattering
    • Mimouni A., Deeth H.C., Whittaker A.K., Gidley M.J., Bhandari B.R. Rehydration process of milk protein concentrate powder monitored by static light scattering. Food Hydrocolloids 2009, 23:1958-1965.
    • (2009) Food Hydrocolloids , vol.23 , pp. 1958-1965
    • Mimouni, A.1    Deeth, H.C.2    Whittaker, A.K.3    Gidley, M.J.4    Bhandari, B.R.5
  • 33
    • 77952694184 scopus 로고    scopus 로고
    • Rehydration of high-protein-containing dairy powder: slow- and fast-dissolving components and storage effects
    • Mimouni A., Deeth H.C., Whittaker A.K., Gidley M.J., Bhandari B.R. Rehydration of high-protein-containing dairy powder: slow- and fast-dissolving components and storage effects. Dairy Science and Technology 2010, 90:335-344.
    • (2010) Dairy Science and Technology , vol.90 , pp. 335-344
    • Mimouni, A.1    Deeth, H.C.2    Whittaker, A.K.3    Gidley, M.J.4    Bhandari, B.R.5
  • 34
    • 77949308270 scopus 로고    scopus 로고
    • Investigation of the microstructure of milk protein concentrate powders during rehydration: alterations during storage
    • Mimouni A., Deeth H.C., Whittaker A.K., Gidley M.J., Bhandari B.R. Investigation of the microstructure of milk protein concentrate powders during rehydration: alterations during storage. Journal of Dairy Science 2010, 93:463-472.
    • (2010) Journal of Dairy Science , vol.93 , pp. 463-472
    • Mimouni, A.1    Deeth, H.C.2    Whittaker, A.K.3    Gidley, M.J.4    Bhandari, B.R.5
  • 35
    • 0036652604 scopus 로고    scopus 로고
    • Manufacture and application of high milk protein powder
    • Mistry V.V. Manufacture and application of high milk protein powder. Lait 2002, 82:515-522.
    • (2002) Lait , vol.82 , pp. 515-522
    • Mistry, V.V.1
  • 36
    • 0030477612 scopus 로고    scopus 로고
    • Physical and storage properties of high milk protein powder
    • Mistry V.V., Pulgar J.B. Physical and storage properties of high milk protein powder. International Dairy Journal 1996, 6:195-203.
    • (1996) International Dairy Journal , vol.6 , pp. 195-203
    • Mistry, V.V.1    Pulgar, J.B.2
  • 37
    • 84974143698 scopus 로고
    • Small-angle X-ray scattering investigation of the micellar and submicellar forms of bovine casein
    • Pessen H., Kumosinski T.F., Farrell H.M. Small-angle X-ray scattering investigation of the micellar and submicellar forms of bovine casein. Journal of Dairy Research 1989, 56:443-451.
    • (1989) Journal of Dairy Research , vol.56 , pp. 443-451
    • Pessen, H.1    Kumosinski, T.F.2    Farrell, H.M.3
  • 39
    • 38849182710 scopus 로고    scopus 로고
    • Scattering and turbidity study of the dissociation of casein by calcium chelation
    • Pitkowski A., Nicolai T., Durand D. Scattering and turbidity study of the dissociation of casein by calcium chelation. Biomacromolecules 2008, 9:369-375.
    • (2008) Biomacromolecules , vol.9 , pp. 369-375
    • Pitkowski, A.1    Nicolai, T.2    Durand, D.3
  • 40
    • 80051585353 scopus 로고    scopus 로고
    • Casein and related products
    • Wiley-Blackwell, Chichester, UK, A.Y. Tamine (Ed.)
    • Rollema H.S., Muir D.D. Casein and related products. Dairy powders and concentrated products 2009, 235-254. Wiley-Blackwell, Chichester, UK. A.Y. Tamine (Ed.).
    • (2009) Dairy powders and concentrated products , pp. 235-254
    • Rollema, H.S.1    Muir, D.D.2
  • 41
    • 2942703853 scopus 로고    scopus 로고
    • Optimization of a nitrogen analyser based on the Dumas method
    • Saint-Denis T., Goupi J. Optimization of a nitrogen analyser based on the Dumas method. Analytica Chimica Acta 2004, 515:191-198.
    • (2004) Analytica Chimica Acta , vol.515 , pp. 191-198
    • Saint-Denis, T.1    Goupi, J.2
  • 42
    • 0042553279 scopus 로고
    • Smoothing and differentiation of data by simplified least squares procedures
    • Savitzky A., Golay M.J.E. Smoothing and differentiation of data by simplified least squares procedures. Analytical Chemistry 1964, 36:1627-1639.
    • (1964) Analytical Chemistry , vol.36 , pp. 1627-1639
    • Savitzky, A.1    Golay, M.J.E.2
  • 44
    • 0033489923 scopus 로고    scopus 로고
    • Dehydration by desorption and by spray-drying of dairy proteins: influence of mineral environment
    • Schuck P., Briard V., Méjean S., Davenel A., Piot M., Famelart M.H., et al. Dehydration by desorption and by spray-drying of dairy proteins: influence of mineral environment. Drying Technology 1999, 17:1347-1357.
    • (1999) Drying Technology , vol.17 , pp. 1347-1357
    • Schuck, P.1    Briard, V.2    Méjean, S.3    Davenel, A.4    Piot, M.5    Famelart, M.H.6
  • 45
    • 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., Méjean S., Piot M. Rehydration of casein powders: effects of added mineral salts and salt addition methods on water transfer. International Dairy Journal 2002, 12:51-57.
    • (2002) International Dairy Journal , vol.12 , pp. 51-57
    • Schuck, P.1    Davenel, A.2    Mariette, F.3    Briard, V.4    Méjean, S.5    Piot, M.6
  • 46
    • 0000820778 scopus 로고
    • Spray-drying of native phosphocaseinate obtained by membrane microfiltration
    • Schuck P., Piat M., Méjean S., Le Graet Y., Fauquant J., Brulé G., et al. Déshydratation par atomisation de phosphocaséinate natif obtenu par microfiltration sur membrane. Lait 1994, 74:375-388.
    • (1994) Lait , vol.74 , pp. 375-388
    • Schuck, P.1    Piat, M.2    Méjean, S.3    Le Graet, Y.4    Fauquant, J.5    Brulé, G.6
  • 47
    • 69249111289 scopus 로고    scopus 로고
    • Structure of casein micelles and their complexation with tannins
    • Shukla A., Narayanan T., Zanchi D. Structure of casein micelles and their complexation with tannins. Soft Matter 2009, 5:2884-2888.
    • (2009) Soft Matter , vol.5 , pp. 2884-2888
    • Shukla, A.1    Narayanan, T.2    Zanchi, D.3
  • 50
    • 0036803243 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins
    • Tompa P. Intrinsically unstructured proteins. Trends in Biochemical Sciences 2002, 27:527-533.
    • (2002) Trends in Biochemical Sciences , vol.27 , pp. 527-533
    • Tompa, P.1
  • 51
    • 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. Journal of Dairy Research 2000, 67:361-370.
    • (2000) Journal of Dairy Research , vol.67 , pp. 361-370
    • Udabage, P.1    McKinnon, I.R.2    Augustin, M.A.3
  • 52
    • 34247206549 scopus 로고    scopus 로고
    • Seasonal variation in milk production and cheese yield from commercial dairy farms located in northern Victoria is associated with pasture and grazing management and supplementary feeding practice
    • Walker G.P., Williams R., Doyle P.T., Dunshea F.R. Seasonal variation in milk production and cheese yield from commercial dairy farms located in northern Victoria is associated with pasture and grazing management and supplementary feeding practice. Australian Journal of Experimental Agriculture 2007, 47:509-524.
    • (2007) Australian Journal of Experimental Agriculture , vol.47 , pp. 509-524
    • Walker, G.P.1    Williams, R.2    Doyle, P.T.3    Dunshea, F.R.4
  • 53
    • 85025797643 scopus 로고
    • On the stability of casein micelles
    • Walstra P. On the stability of casein micelles. Journal of Dairy Science 1990, 73:1965-1979.
    • (1990) Journal of Dairy Science , vol.73 , pp. 1965-1979
    • Walstra, P.1
  • 54
    • 0032818601 scopus 로고    scopus 로고
    • Casein submicelles: do they exist?
    • Walstra P. Casein submicelles: do they exist?. International Dairy Journal 1999, 9:189-192.
    • (1999) International Dairy Journal , vol.9 , pp. 189-192
    • Walstra, P.1
  • 55
    • 1442335307 scopus 로고    scopus 로고
    • Effect of pH and ionic strength on competitive protein adsorption to air/water interfaces in aqueous foams made with mixed proteins
    • Zhang Z., Dalgleish D.G., Goff H.D. Effect of pH and ionic strength on competitive protein adsorption to air/water interfaces in aqueous foams made with mixed proteins. Colloid and Surface B: Biointerfaces 2004, 34:113-121.
    • (2004) Colloid and Surface B: Biointerfaces , vol.34 , pp. 113-121
    • Zhang, Z.1    Dalgleish, D.G.2    Goff, H.D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.