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Volumn 88, Issue 1, 2008, Pages 121-147

Role of protein aggregation in heat-induced heat stability during milk powder manufacture

Author keywords

Heat stability; Micellar integrity; Milk protein aggregation

Indexed keywords


EID: 41849088866     PISSN: 19585586     EISSN: 19585594     Source Type: Journal    
DOI: 10.1051/dst:2007048     Document Type: Article
Times cited : (17)

References (41)
  • 1
    • 84919233874 scopus 로고
    • Standards for grades of dry milks including methods of analysis
    • American Dry Milk Institute, American Dry Milk Institute, Chicago
    • American Dry Milk Institute, Standards for grades of dry milks including methods of analysis, Bulletin 916, American Dry Milk Institute, Chicago (1971) p. 9.
    • (1971) Bulletin , vol.916 , pp. 9
  • 2
    • 21744454059 scopus 로고    scopus 로고
    • The effect of pH and heat treatments on the K-casein content and the ζ potential of the particles in reconstituted skim milk
    • Anema S.G., Klostermeyer H., The effect of pH and heat treatments on the K-casein content and the ζ potential of the particles in reconstituted skim milk, Milchwissenschaft 52 (1997) 217-222.
    • (1997) Milchwissenschaft , vol.52 , pp. 217-222
    • Anema, S.G.1    Klostermeyer, H.2
  • 3
    • 0001233557 scopus 로고    scopus 로고
    • Further studies on the heat-induced pH dependent dissociation of casein from the micelles in reconstituted skim milk
    • Anema S.G., Li Y., Further studies on the heat-induced pH dependent dissociation of casein from the micelles in reconstituted skim milk, Lebensm.-Wiss. Technol. 33 (2000) 335-343.
    • (2000) Lebensm.-Wiss. Technol , vol.33 , pp. 335-343
    • Anema, S.G.1    Li, Y.2
  • 4
    • 0037324448 scopus 로고    scopus 로고
    • Association of denatured whey proteins with casein micelles in heated reconstituted skim milk and its effect on casein micelle size
    • Anema S., Li Y., Association of denatured whey proteins with casein micelles in heated reconstituted skim milk and its effect on casein micelle size, J. Dairy Res. 70 (2003) 73-83.
    • (2003) J. Dairy Res , vol.70 , pp. 73-83
    • Anema, S.1    Li, Y.2
  • 6
    • 84976004027 scopus 로고
    • Effects of added salts on the heat stability of recombined concentrated milk
    • Augustin M.A., Clarke P.T., Effects of added salts on the heat stability of recombined concentrated milk, J. Dairy Res. 57 (1990) 213-226.
    • (1990) J. Dairy Res , vol.57 , pp. 213-226
    • Augustin, M.A.1    Clarke, P.T.2
  • 7
    • 84974450815 scopus 로고
    • Calcium ion activities of cooled and aged reconstituted recombined milks
    • Augustin M.A., Clarke P.T., Calcium ion activities of cooled and aged reconstituted recombined milks, J. Dairy Res. 58 (1991) 219-229.
    • (1991) J. Dairy Res , vol.58 , pp. 219-229
    • Augustin, M.A.1    Clarke, P.T.2
  • 8
    • 0005076083 scopus 로고
    • The heat stability of recombined evaporated milk made from skim milk powder produced in late autumn and winter
    • Augustin M.A., Clarke P.T., Greenwood T., The heat stability of recombined evaporated milk made from skim milk powder produced in late autumn and winter, Aust. J. Dairy Technol. 45 (1990) 47-49.
    • (1990) Aust. J. Dairy Technol , vol.45 , pp. 47-49
    • Augustin, M.A.1    Clarke, P.T.2    Greenwood, T.3
  • 9
    • 0033858518 scopus 로고    scopus 로고
    • Thermal denaturation of mixtures of a-lactalbumin and β-lactalbumin: A differential scanning calorimetric study
    • Boye J.I., Alli L, Thermal denaturation of mixtures of a-lactalbumin and β-lactalbumin: A differential scanning calorimetric study, Food Res. Int. 33 (2000) 673-682.
    • (2000) Food Res. Int , vol.33 , pp. 673-682
    • Boye, J.I.1    Alli, L.2
  • 10
    • 41849145975 scopus 로고    scopus 로고
    • CODEX STAN 207-1999: Codex standard for milk powders and cream powder, viewed on line, 20 March 2007, http://www.codexalimentarius.net/download/ standards/333/CXS_207e.pdf.
    • CODEX STAN 207-1999: Codex standard for milk powders and cream powder, viewed on line, 20 March 2007, http://www.codexalimentarius.net/download/ standards/333/CXS_207e.pdf.
  • 11
    • 0000286380 scopus 로고    scopus 로고
    • The binding of α-lactalbumin and β-lactoglobulin to casein micelles in milk treated by differing heating systems
    • Corredig M., Dalgleish D.G., The binding of α-lactalbumin and β-lactoglobulin to casein micelles in milk treated by differing heating systems, Milchwissenschaft 51 (1996) 123-126.
    • (1996) Milchwissenschaft , vol.51 , pp. 123-126
    • Corredig, M.1    Dalgleish, D.G.2
  • 12
    • 0032867758 scopus 로고    scopus 로고
    • The mechanisms of the heat-induced interaction of whey proteins with casein micelles in milk
    • Corredig M., Dalgleish D.G., The mechanisms of the heat-induced interaction of whey proteins with casein micelles in milk, Int. Dairy J. 9 (1999) 233-236.
    • (1999) Int. Dairy J , vol.9 , pp. 233-236
    • Corredig, M.1    Dalgleish, D.G.2
  • 13
    • 84974514610 scopus 로고
    • Studies on the heat stability of milk I. Behaviour of divalent cations and phosphate in milk heated in a stainless steel system
    • Dalgleish D.G., Pouliot Y., Paquin P., Studies on the heat stability of milk I. Behaviour of divalent cations and phosphate in milk heated in a stainless steel system, J. Dairy Res. 54 (1987) 29-37.
    • (1987) J. Dairy Res , vol.54 , pp. 29-37
    • Dalgleish, D.G.1    Pouliot, Y.2    Paquin, P.3
  • 14
    • 84987367516 scopus 로고
    • Reaction kinetics of the denaturation of whey proteins in milk
    • Dannenberg F., Kessler H.-G., Reaction kinetics of the denaturation of whey proteins in milk, J. Food Sci. 53 (1988) 258-263.
    • (1988) J. Food Sci , vol.53 , pp. 258-263
    • Dannenberg, F.1    Kessler, H.-G.2
  • 15
    • 84972090718 scopus 로고
    • Heat stability of milk
    • Darling D.F., Heat stability of milk, J. Dairy Res. 47 (1980) 199-210.
    • (1980) J. Dairy Res , vol.47 , pp. 199-210
    • Darling, D.F.1
  • 16
    • 84986481276 scopus 로고
    • The relations of temperature and time of forewarming of milk to the heat stability of its evaporated product
    • Deysher E.F., Webb B.H., Holm G.E., The relations of temperature and time of forewarming of milk to the heat stability of its evaporated product, J. Dairy Sci. 12 (1929) 80-89.
    • (1929) J. Dairy Sci , vol.12 , pp. 80-89
    • Deysher, E.F.1    Webb, B.H.2    Holm, G.E.3
  • 17
    • 33750471143 scopus 로고    scopus 로고
    • Effect of the heating pH on the qualitative and quantitative compositions of the sera of reconstituted skim milks and on the mechanisms of formation of soluble aggregates
    • Donato L., Dalgleish D.G., Effect of the heating pH on the qualitative and quantitative compositions of the sera of reconstituted skim milks and on the mechanisms of formation of soluble aggregates, J. Agric. Food Chem. 54 (2006) 7804-7811.
    • (2006) J. Agric. Food Chem , vol.54 , pp. 7804-7811
    • Donato, L.1    Dalgleish, D.G.2
  • 18
    • 0041802887 scopus 로고    scopus 로고
    • Formation of soluble and micelle-bound aggregates in heated milk
    • Guyomarc'h F., Law A.J.L., Dalgleish D.G., Formation of soluble and micelle-bound aggregates in heated milk, J. Agric. Food Chem. 51 (2003) 4652-4660.
    • (2003) J. Agric. Food Chem , vol.51 , pp. 4652-4660
    • Guyomarc'h, F.1    Law, A.J.L.2    Dalgleish, D.G.3
  • 19
    • 0039835204 scopus 로고    scopus 로고
    • Effect of protein standardization of milk by addition of UF milk permeate on the composition and storage stability of UHT processed milk
    • Hardham J.F., Effect of protein standardization of milk by addition of UF milk permeate on the composition and storage stability of UHT processed milk, Aust. J. Dairy Technol. 53 (1998) 22-27.
    • (1998) Aust. J. Dairy Technol , vol.53 , pp. 22-27
    • Hardham, J.F.1
  • 20
    • 0019564975 scopus 로고
    • Calculation of the ion equilibria in milk diffusate and comparison with, experiment
    • Holt C., Dalgleish D.G., Jenness R., Calculation of the ion equilibria in milk diffusate and comparison with, experiment, Anal. Biochem. 113 (1981) 154-163.
    • (1981) Anal. Biochem , vol.113 , pp. 154-163
    • Holt, C.1    Dalgleish, D.G.2    Jenness, R.3
  • 21
    • 0036866003 scopus 로고    scopus 로고
    • Casein structure, self assembly and gelation
    • Home D.S., Casein structure, self assembly and gelation, Curr. Opin. Colloid Interface Sci. 7 (2002) 456-461.
    • (2002) Curr. Opin. Colloid Interface Sci , vol.7 , pp. 456-461
    • Home, D.S.1
  • 22
    • 30344474283 scopus 로고    scopus 로고
    • Structure and surface properties of the serum heat-induced protein aggregates isolated from heated skim milk
    • Jean K., Renan M., Famelart M.-H., Guyomarc'h F., Structure and surface properties of the serum heat-induced protein aggregates isolated from heated skim milk, Int. Dairy J. 16 (2006) 303-315.
    • (2006) Int. Dairy J , vol.16 , pp. 303-315
    • Jean, K.1    Renan, M.2    Famelart, M.-H.3    Guyomarc'h, F.4
  • 23
    • 0030511662 scopus 로고    scopus 로고
    • Effect of disaccharides on the thermal properties of whey proteins determined by differential scanning calorimetry (DSC)
    • Jou K.D., Harper W.J., Effect of disaccharides on the thermal properties of whey proteins determined by differential scanning calorimetry (DSC), Milchwissenschaft 51 (1996) 509-512.
    • (1996) Milchwissenschaft , vol.51 , pp. 509-512
    • Jou, K.D.1    Harper, W.J.2
  • 24
    • 0040617829 scopus 로고
    • An objective method for the determination of heat stability of milk powders
    • Kieseker F.G., Aitken B., An objective method for the determination of heat stability of milk powders, Aust. J. Dairy Technol. 43 (1988) 26-31.
    • (1988) Aust. J. Dairy Technol , vol.43 , pp. 26-31
    • Kieseker, F.G.1    Aitken, B.2
  • 25
    • 0026566944 scopus 로고
    • Glutamate dehydrogenase from the hyperthermophile Pyrococcus furiosus: Thermal denaturation and activation
    • Klump H., DiRuggiero J., Kessel M., Park J.-B., Adams M.W.W., Robb F.T., Glutamate dehydrogenase from the hyperthermophile Pyrococcus furiosus: Thermal denaturation and activation, J. Biol. Chem. 267 (1992) 22681-22685.
    • (1992) J. Biol. Chem , vol.267 , pp. 22681-22685
    • Klump, H.1    DiRuggiero, J.2    Kessel, M.3    Park, J.-B.4    Adams, M.W.W.5    Robb, F.T.6
  • 26
    • 41849117597 scopus 로고    scopus 로고
    • Newstead D.F., Sanderson W.B., Bauke A.G., The effects of heat treatment and pH on the heat stability of recombined evaporated milk, N.Z.J. Dairy Sci. Technol. 10 (1975) 113-118.
    • Newstead D.F., Sanderson W.B., Bauke A.G., The effects of heat treatment and pH on the heat stability of recombined evaporated milk, N.Z.J. Dairy Sci. Technol. 10 (1975) 113-118.
  • 27
    • 84985200386 scopus 로고
    • Radiolabelling study of the heat-induced interactions between alpha-lactalbumin, betalactoglobulin and kappa-casein in milk and in buffer solutions
    • Noh B., Richardson T., Creamer L.K., Radiolabelling study of the heat-induced interactions between alpha-lactalbumin, betalactoglobulin and kappa-casein in milk and in buffer solutions, J. Food Sci. 54 (1989) 889-893.
    • (1989) J. Food Sci , vol.54 , pp. 889-893
    • Noh, B.1    Richardson, T.2    Creamer, L.K.3
  • 28
    • 0034150548 scopus 로고    scopus 로고
    • The two-stage coagulation of milk proteins in the minimum, of the heat coagulation time-pH profile of milk: Effect of casein micelle size
    • O'Connell J.E., Fox P.F., The two-stage coagulation of milk proteins in the minimum, of the heat coagulation time-pH profile of milk: Effect of casein micelle size, J. Dairy Sci. 83 (2000) 378-386.
    • (2000) J. Dairy Sci , vol.83 , pp. 378-386
    • O'Connell, J.E.1    Fox, P.F.2
  • 29
    • 0033668026 scopus 로고    scopus 로고
    • Heat-induced interactions of β-lactoglobulin and α-lactalbumin with, the casein micelle in pH adjusted skim milk
    • Oldfield D.J., Singh H., Taylor M.W., Pearce K.N., Heat-induced interactions of β-lactoglobulin and α-lactalbumin with, the casein micelle in pH adjusted skim milk, Int. Dairy J. 10 (2000) 509-518.
    • (2000) Int. Dairy J , vol.10 , pp. 509-518
    • Oldfield, D.J.1    Singh, H.2    Taylor, M.W.3    Pearce, K.N.4
  • 30
    • 0002295609 scopus 로고
    • Observations on the seasonal variation in the salt balance of concentrated milk
    • Pouliot Y., Boulet M., Observations on the seasonal variation in the salt balance of concentrated milk, Int. Dairy J. 5 (1995) 75-85.
    • (1995) Int. Dairy J , vol.5 , pp. 75-85
    • Pouliot, Y.1    Boulet, M.2
  • 33
    • 32544451336 scopus 로고    scopus 로고
    • Structures and some properties of soluble protein complexes formed by the heating of reconstituted skim milk powder
    • Rodriguez del Angel C., Dalgleish D.G., Structures and some properties of soluble protein complexes formed by the heating of reconstituted skim milk powder, Food Res. Int. 39 (2006) 472-479.
    • (2006) Food Res. Int , vol.39 , pp. 472-479
    • Rodriguez del Angel, C.1    Dalgleish, D.G.2
  • 34
    • 84974200389 scopus 로고
    • Influence of concentration of milk solids on the dissociation of micellar κ-casein on heating reconstituted milk at 120° C
    • Singh H., Creamer L.K., Influence of concentration of milk solids on the dissociation of micellar κ-casein on heating reconstituted milk at 120° C, J. Dairy Res. 58 (1991) 99-105.
    • (1991) J. Dairy Res , vol.58 , pp. 99-105
    • Singh, H.1    Creamer, L.K.2
  • 35
    • 84985200254 scopus 로고
    • Aggregation and dissociation of milk protein complexes in heated reconstituted concentrated skim milks
    • Singh H., Creamer L.K., Aggregation and dissociation of milk protein complexes in heated reconstituted concentrated skim milks, J. Food Sci. 56 (1991) 238-246.
    • (1991) J. Food Sci , vol.56 , pp. 238-246
    • Singh, H.1    Creamer, L.K.2
  • 36
    • 0001876853 scopus 로고
    • Heat stability of milk: PH-dependent dissociation of micellar κ-casein on heating milk at ultra high temperatures
    • Singh H., Fox P.F., Heat stability of milk: pH-dependent dissociation of micellar κ-casein on heating milk at ultra high temperatures, J. Dairy Res. 52 (1985) 529-538.
    • (1985) J. Dairy Res , vol.52 , pp. 529-538
    • Singh, H.1    Fox, P.F.2
  • 37
    • 0001347880 scopus 로고
    • Heat stability of milk: Aggregation and dissociation of protein at ultra high temperatures
    • Singh H., Latham J., Heat stability of milk: Aggregation and dissociation of protein at ultra high temperatures, Int. Dairy J. 3 (1993) 22-237.
    • (1993) Int. Dairy J , vol.3 , pp. 22-237
    • Singh, H.1    Latham, J.2
  • 38
    • 0041352838 scopus 로고    scopus 로고
    • Quantification of heat-induced casein-whey protein interactions in milk, and its relation to gelation kinetics
    • Vasbinder A.J., Alting A.C., deKruif K.G., Quantification of heat-induced casein-whey protein interactions in milk, and its relation to gelation kinetics, Colloid Surf. B 31 (2003) 115-123.
    • (2003) Colloid Surf. B , vol.31 , pp. 115-123
    • Vasbinder, A.J.1    Alting, A.C.2    deKruif, K.G.3
  • 39
    • 0043241649 scopus 로고    scopus 로고
    • Casein whey interactions in heated milk: The influence of pH
    • Vasbinder A.J., deKruif K.G., Casein whey interactions in heated milk: the influence of pH, Int. Dairy J. 13 (2003) 669-777.
    • (2003) Int. Dairy J , vol.13 , pp. 669-777
    • Vasbinder, A.J.1    deKruif, K.G.2
  • 40
    • 23044532492 scopus 로고    scopus 로고
    • The relationship between the composition of milk and the properties of bulk milk products
    • Williams R.P.W., The relationship between the composition of milk and the properties of bulk milk products, Aust. J. Dairy Technol. 57 (2002) 30-44.
    • (2002) Aust. J. Dairy Technol , vol.57 , pp. 30-44
    • Williams, R.P.W.1
  • 41
    • 25144508243 scopus 로고    scopus 로고
    • Production of calcium-fortified milk, powders using soluble calcium salts
    • Williams R.P.W., D'Ath L., Augustin M.A., Production of calcium-fortified milk, powders using soluble calcium salts, Lait 85 (2005) 369-381.
    • (2005) Lait , vol.85 , pp. 369-381
    • Williams, R.P.W.1    D'Ath, L.2    Augustin, M.A.3


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