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Volumn , Issue , 2016, Pages 179-196

Heat stability of milk

Author keywords

Calcium; Casein dissociation; Heat stability; Lactose hydrolysis; Milk; Whey protein denaturation

Indexed keywords

CALCIUM; CASEIN; COAGULATION; DENATURATION; DISSOCIATION; MICELLES; PROTEINS; STABILITY; SUGARS; UREA;

EID: 84956726298     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1007/978-1-4939-2800-2_7     Document Type: Chapter
Times cited : (81)

References (98)
  • 1
    • 0000290017 scopus 로고    scopus 로고
    • Effect of milk concentration on heat- induced, ph-dependent dissociation of casein from micelles in reconstituted skim milk at temperatures between 20 and 120°c
    • Anema SG (1998) Effect of milk concentration on heat- induced, pH-dependent dissociation of casein from micelles in reconstituted skim milk at temperatures between 20 and 120°C. J Agric Food Chem 46:2299-2305
    • (1998) J Agric Food Chem , vol.46 , pp. 2299-2305
    • Anema, S.G.1
  • 2
    • 0033805350 scopus 로고    scopus 로고
    • Effect of milk concentration on the irreversible thermal denaturation and disulfide aggregation of p-lactoglobulin
    • Anema SG (2000) Effect of milk concentration on the irreversible thermal denaturation and disulfide aggregation of p-lactoglobulin. J Agric Food Chem 48:4168-4175
    • (2000) J Agric Food Chem , vol.48 , pp. 4168-4175
    • Anema, S.G.1
  • 3
    • 0035076309 scopus 로고    scopus 로고
    • Kinetics of the irreversible thermal denaturation and disulfide aggregation of a-lactalbu- min in milk samples of various concentrations
    • Anema SG (2001) Kinetics of the irreversible thermal denaturation and disulfide aggregation of a-lactalbu- min in milk samples of various concentrations. J Food Sci 66:2-9
    • (2001) J Food Sci , vol.66 , pp. 2-9
    • Anema, S.G.1
  • 4
    • 34249329941 scopus 로고    scopus 로고
    • Role of k-casein in the association of denatured whey proteins with casein micelles in heated reconstituted skim milk
    • Anema SG (2007) Role of K-casein in the association of denatured whey proteins with casein micelles in heated reconstituted skim milk. J Agric Food Chem 55:3635-3642
    • (2007) J Agric Food Chem , vol.55 , pp. 3635-3642
    • Anema, S.G.1
  • 5
    • 75149129165 scopus 로고    scopus 로고
    • The whey proteins in milk: Thermal denaturation, physical interactions and effects on the functional properties of milk
    • Thompson A, Boland M, Singh H, Academic/Elsevier, Amsterdam
    • Anema SG (2009) The whey proteins in milk: thermal denaturation, physical interactions and effects on the functional properties of milk. In: Thompson A, Boland M, Singh H (eds) Milk proteins: from expression to food. Academic/Elsevier, Amsterdam, pp 239-281
    • (2009) Milk Proteins: From Expression to Food , pp. 239-281
    • Anema, S.G.1
  • 6
    • 0000011321 scopus 로고    scopus 로고
    • Heat-induced, ph- dependent dissociation of casein micelles on heating reconstituted skim milk at temperatures below 100°c
    • Anema SG, Klostermeyer H (1997) Heat-induced, pH- dependent dissociation of casein micelles on heating reconstituted skim milk at temperatures below 100°C. J Agric Food Chem 45:1108-1115
    • (1997) J Agric Food Chem , vol.45 , pp. 1108-1115
    • Anema, S.G.1    Klostermeyer, H.2
  • 7
    • 0001430290 scopus 로고    scopus 로고
    • ) reaction kinetics of thermal denaturation of whey proteins in heated reconstituted whole milk
    • Anema SG, McKenna AB (1996) Reaction kinetics of thermal denaturation of whey proteins in heated reconstituted whole milk. J Agric Food Chem 44:422-428
    • (1996) J Agric Food Chem , vol.44 , pp. 422-428
    • Anema, S.G.1    Mc Kenna, A.B.2
  • 9
    • 3843144836 scopus 로고    scopus 로고
    • Effect of ph at heating on the acid-induced aggregation of casein micelles in reconstituted skim milk
    • Anema SG, Lowe EK, Lee SK (2004) Effect of pH at heating on the acid-induced aggregation of casein micelles in reconstituted skim milk. Lebensm Wiss Technol-Food Sci Technol 37:779-787
    • (2004) Lebensm Wiss Technol-Food Sci Technol , vol.37 , pp. 779-787
    • Anema, S.G.1    Lowe, E.K.2    Lee, S.K.3
  • 10
    • 84954913864 scopus 로고
    • Effect of formaldehyde on the heat stability of concentrated milk and the formation of soluble casein
    • Aoki T, Kako Y (1984) Effect of formaldehyde on the heat stability of concentrated milk and the formation of soluble casein. Agric Biol Chem 48:1017-1021
    • (1984) Agric Biol Chem , vol.48 , pp. 1017-1021
    • Aoki, T.1    Kako, Y.2
  • 11
    • 84976004027 scopus 로고
    • Effects of added salts on the heat stability of recombined concentrated milk
    • Augustin MA, Clarke PT (1990) Effects of added salts on the heat stability of recombined concentrated milk. J Dairy Res 57:213-226
    • (1990) J Dairy Res , vol.57 , pp. 213-226
    • Augustin, M.A.1    Clarke, P.T.2
  • 13
    • 0001826539 scopus 로고
    • Dephosphorization of casein by heat treatment
    • Belec J, Jenness R (1962b) Dephosphorization of casein by heat treatment. II. In skim milks. J Dairy Sci 45:20-26
    • (1962) Skim Milks. J Dairy Sci , vol.45 , pp. 20-26
    • Belec, J.1    Jenness, R.2
  • 14
    • 0000611410 scopus 로고
    • Degradation of lactose during heating of milk. 1. Reaction pathways
    • Berg HE, van Boekel MAJS (1994) Degradation of lactose during heating of milk. 1. Reaction pathways. Neth Milk Dairy J 48:157-175
    • (1994) Neth Milk Dairy J , vol.48 , pp. 157-175
    • Berg, H.E.1    Van Boekel, M.2
  • 15
    • 77957323668 scopus 로고    scopus 로고
    • The influence of milk composition on ph and calcium activity measured in situ during heat treatment of reconstituted skim milk
    • Chandrapala J, McKinnon I, Augustin MA, Udabage P (2010) The influence of milk composition on pH and calcium activity measured in situ during heat treatment of reconstituted skim milk. J Dairy Res 77:257-264
    • (2010) J Dairy Res , vol.77 , pp. 257-264
    • Chandrapala, J.1    Mc Kinnon, I.2    Augustin, M.A.3    Udabage, P.4
  • 16
    • 84976130764 scopus 로고
    • Effect of temperature on the ph of skim milk
    • Chaplin LC, Lyster RLJ (1988) Effect of temperature on the pH of skim milk. J Dairy Res 55:277-280
    • (1988) J Dairy Res , vol.55 , pp. 277-280
    • Chaplin, L.C.1    Lyster, R.2
  • 17
    • 0001941841 scopus 로고
    • The enzymatic coagulation of milk
    • Fox PF, 2nd edn. Chapman & Hall, London
    • Dalgleish DG (1993) The enzymatic coagulation of milk. In: Fox PF (ed) Cheese: chemistry, physics and microbiology, 2nd edn. Chapman & Hall, London, pp 69-100
    • (1993) Cheese: Chemistry, Physics and Microbiology , pp. 69-100
    • Dalgleish, D.G.1
  • 18
    • 79952381343 scopus 로고    scopus 로고
    • On the structural models of bovine casein micelles and possible improvements
    • Dalgleish DG (2011) On the structural models of bovine casein micelles and possible improvements. Soft Matter 7:2265-2272
    • (2011) Soft Matter , vol.7 , pp. 2265-2272
    • Dalgleish, D.G.1
  • 19
    • 84974326090 scopus 로고
    • Studies on the heat stability of milk. Ii. Association and dissociation of particles and the effect of added urea
    • Dalgleish DG, Pouliot Y, Paquin P (1987) Studies on the heat stability of milk. II. Association and dissociation of particles and the effect of added urea. J Dairy Res 54:39-49
    • (1987) J Dairy Res , vol.54 , pp. 39-49
    • Dalgleish, D.G.1    Pouliot, Y.2    Paquin, P.3
  • 20
    • 4544282070 scopus 로고    scopus 로고
    • A possible structure of the casein micelles based on highresolution scanning electron microscopy
    • Dalgleish DG, Spagnuolo P, Goff HD (2004) A possible structure of the casein micelles based on highresolution scanning electron microscopy. Int Dairy J 14:1025-1031
    • (2004) Int Dairy J , vol.14 , pp. 1025-1031
    • Dalgleish, D.G.1    Spagnuolo, P.2    Goff, H.D.3
  • 21
    • 84987367516 scopus 로고
    • Reaction kinetics of the denaturation of whey proteins in milk
    • Dannenberg F, Kessler HG (1988) Reaction kinetics of the denaturation of whey proteins in milk. J Food Sci 53:258-263
    • (1988) J Food Sci , vol.53 , pp. 258-263
    • Dannenberg, F.1    Kessler, H.G.2
  • 22
    • 84972090718 scopus 로고
    • Heat stability of milk
    • Darling DF (1980) Heat stability of milk. J Dairy Res 47:119-210
    • (1980) J Dairy Res , vol.47 , pp. 119-210
    • Darling, D.F.1
  • 23
    • 0002749539 scopus 로고
    • The stability of milk protein to heat. I. Subjective measurement of heat stability of milk
    • Davies DT, White JCD (1966) The stability of milk protein to heat. I. Subjective measurement of heat stability of milk. J Dairy Res 33:67-81
    • (1966) J Dairy Res , vol.33 , pp. 67-81
    • Davies, D.T.1    White, J.2
  • 24
    • 0032839313 scopus 로고    scopus 로고
    • Casein micelle interactions
    • De Kruif CG (1999) Casein micelle interactions. Int Dairy J 9:183-188
    • (1999) Int Dairy J , vol.9 , pp. 183-188
    • De Kruif, C.G.1
  • 25
    • 0348114294 scopus 로고    scopus 로고
    • Casein micelle structure, functions and interactions
    • Fox PF, McSweeney PLH, 3rd edn, Proteins. Kluwer Academic/Plenum, New York
    • De Kruif CG, Holt C (2003) Casein micelle structure, functions and interactions. In: Fox PF, McSweeney PLH (eds) Advanced dairy chemistry, vol 1, 3rd edn, Proteins. Kluwer Academic/Plenum, New York, pp 233-270
    • (2003) Advanced Dairy Chemistry , vol.1 , pp. 233-270
    • De Kruif, C.G.1    Holt, C.2
  • 26
    • 0030588089 scopus 로고    scopus 로고
    • K-casein as a polyelectrolyte brush on the surface of casein micelles
    • De Kruif CG, Zhulina EB (1996) K-casein as a polyelectrolyte brush on the surface of casein micelles. Colloids Surface A 117:151-159
    • (1996) Colloids Surface A , vol.117 , pp. 151-159
    • De Kruif, C.G.1    Zhulina, E.B.2
  • 28
    • 33645477666 scopus 로고
    • Klaro- graph: A new approach for measurement of the viscosity, density and heat stability in milk and milk concentrates at temperatures up to 140°c
    • De Wit JN, Klarenbeek G, de Graaf C (1986) Klaro- graph: a new approach for measurement of the viscosity, density and heat stability in milk and milk concentrates at temperatures up to 140°C. Voedingsm iddelentechnologie 6:25-27
    • (1986) Voedingsm Iddelentechnologie , vol.6 , pp. 25-27
    • De Wit, J.N.1    Klarenbeek, G.2    De Graaf, C.3
  • 29
    • 27544482293 scopus 로고
    • An automatic method for measuring the heat coagulation time of milk powder solutions
    • Foissy H, Kneifel W (1984) An automatic method for measuring the heat coagulation time of milk powder solutions. J Dairy Res 51:325-329
    • (1984) J Dairy Res , vol.51 , pp. 325-329
    • Foissy, H.1    Kneifel, W.2
  • 30
    • 0343939558 scopus 로고
    • Heat stability of milk: The significance of heat-induced acid formation in coagulation
    • Fox PF (1981) Heat stability of milk: the significance of heat-induced acid formation in coagulation. Irish J Food Sci Technol 5:1-11
    • (1981) Irish J Food Sci Technol , vol.5 , pp. 1-11
    • Fox, P.F.1
  • 31
    • 0002266872 scopus 로고
    • Heat-induced coagulation of milk
    • Fox PF, Applied Science, London
    • Fox PF (1982) Heat-induced coagulation of milk. In: Fox PF (ed) Developments in dairy chemistry-I, Proteins. Applied Science, London, pp 189-228
    • (1982) Developments in Dairy Chemistry-I, Proteins , pp. 189-228
    • Fox, P.F.1
  • 32
    • 84976164399 scopus 로고
    • Reviews of the progress of dairy science: The heat stability of milk
    • Fox PF, Morrissey PA (1977) Reviews of the progress of dairy science: the heat stability of milk. J Dairy Res 44:627-646
    • (1977) J Dairy Res , vol.44 , pp. 627-646
    • Fox, P.F.1    Morrissey, P.A.2
  • 34
    • 0026668858 scopus 로고
    • Structure and stability of bovine casein micelles
    • Holt C (1992) Structure and stability of bovine casein micelles. Adv Protein Chem 43:63-151
    • (1992) Adv Protein Chem , vol.43 , pp. 63-151
    • Holt, C.1
  • 35
    • 0001871181 scopus 로고    scopus 로고
    • The hairy casein micelle: Evolution of the concept and its implications for dairy technology
    • Holt C, Horne DS (1996) The hairy casein micelle: evolution of the concept and its implications for dairy technology. Neth Milk Dairy J 50:85-111
    • (1996) Neth Milk Dairy J , vol.50 , pp. 85-111
    • Holt, C.1    Horne, D.S.2
  • 36
    • 84972015936 scopus 로고
    • Seasonal changes in the heat stability of milk from creamery silos in south-west scotland
    • Holt C, Muir DD, Sweetsur AM (1978a) Seasonal changes in the heat stability of milk from creamery silos in south-west Scotland. J Dairy Res 45:183-190
    • (1978) J Dairy Res , vol.45 , pp. 183-190
    • Holt, C.1    Muir, D.D.2    Sweetsur, A.M.3
  • 37
    • 0013473473 scopus 로고
    • The heat stability of milk and concentrated milk containing added aldehydes and sugars
    • Holt C, Muir DD, Sweetsur AWM (1978b) The heat stability of milk and concentrated milk containing added aldehydes and sugars. J Dairy Res 45:47-52
    • (1978) J Dairy Res , vol.45 , pp. 47-52
    • Holt, C.1    Muir, D.D.2    Sweetsur, A.3
  • 38
    • 84884353426 scopus 로고    scopus 로고
    • Caseins and the casein micelle: Their biological functions, structures, and behavior in foods
    • Holt C, Carver JA, Ecroyd H, Thorn DC (2013) Caseins and the casein micelle: their biological functions, structures, and behavior in foods. J Dairy Sci 96:6127-6146
    • (2013) J Dairy Sci , vol.96 , pp. 6127-6146
    • Holt, C.1    Carver, J.A.2    Ecroyd, H.3    Thorn, D.C.4
  • 39
    • 0032029213 scopus 로고    scopus 로고
    • Casein interactions: Casting light on the black boxes, the structure of dairy products
    • Horne DS (1998) Casein interactions: casting light on the black boxes, the structure of dairy products. Int Dairy J 8:171-177
    • (1998) Int Dairy J , vol.8 , pp. 171-177
    • Horne, D.S.1
  • 40
    • 0012856735 scopus 로고    scopus 로고
    • Ethanol stability
    • Fox PF, McSweeney PLH (eds) Advanced dairy chemistry, vol 1, 3rd edn, Proteins, New York
    • Horne DS (2003) Ethanol stability. In: Fox PF, McSweeney PLH (eds) Advanced dairy chemistry, vol 1, 3rd edn, Proteins. Kluwer Academic/Plenum, New York, pp 975-999
    • (2003) Kluwer Academic/Plenum , pp. 975-999
    • Horne, D.S.1
  • 42
    • 84858756599 scopus 로고    scopus 로고
    • Mineral partitioning in milk and milk permeates at high temperature
    • Kaombe DD, Du Y, Lewis MJ (2012) Mineral partitioning in milk and milk permeates at high temperature. J Dairy Res 79:1-6
    • (2012) J Dairy Res , vol.79 , pp. 1-6
    • Kaombe, D.D.1    Du, Y.2    Lewis, M.J.3
  • 43
    • 0039873623 scopus 로고
    • Studies of milk composition and its relationship to some processing criteria. Iii. Seasonal variation in heat stability of milk
    • Kelly PM, OKeefe AM, Keogh MK, Phelan JA (1982) Studies of milk composition and its relationship to some processing criteria. III. Seasonal variation in heat stability of milk. Irish J Food Sci Technol 6:29-38
    • (1982) Irish J Food Sci Technol , vol.6 , pp. 29-38
    • Kelly, P.M.1    O Keefe, A.M.2    Keogh, M.K.3    Phelan, J.A.4
  • 44
    • 0040617829 scopus 로고
    • An objective method for determination of heat stability of milk powders
    • Kieseker FG, Aitken B (1988) An objective method for determination of heat stability of milk powders. Aust J Dairy Technol 43:26-31
    • (1988) Aust J Dairy Technol , vol.43 , pp. 26-31
    • Kieseker, F.G.1    Aitken, B.2
  • 45
    • 0001313867 scopus 로고
    • The heat stability of milk: Formation of soluble proteins and protein-depleted micelles at elevated temperatures
    • Kudo S (1980a) The heat stability of milk: formation of soluble proteins and protein-depleted micelles at elevated temperatures. NZ J Dairy Sci Technol 15:255-263
    • (1980) NZ J Dairy Sci Technol , vol.15 , pp. 255-263
    • Kudo, S.1
  • 46
    • 0040295088 scopus 로고
    • Influence oflactose and urea on the heat stability of artificial milk systems
    • Kudo S (1980b) Influence oflactose and urea on the heat stability of artificial milk systems. NZ J Dairy Sci Technol15:197-200
    • (1980) NZ J Dairy Sci Technol15 , pp. 197-200
    • Kudo, S.1
  • 47
    • 0034030911 scopus 로고    scopus 로고
    • Effect of ph on the thermal denaturation of whey proteins in milk
    • Law AJ, Leaver J (2000) Effect of pH on the thermal denaturation of whey proteins in milk. J Agric Food Chem 48:672-679
    • (2000) J Agric Food Chem , vol.48 , pp. 672-679
    • Law, A.J.1    Leaver, J.2
  • 48
    • 27544453010 scopus 로고    scopus 로고
    • Determination of the heat stability profiles of concentrated milk and milk ingredients using high resolution ultrasonic spectroscopy
    • Lehmann L, Buckin V (2005) Determination of the heat stability profiles of concentrated milk and milk ingredients using high resolution ultrasonic spectroscopy. J Dairy Sci 88:3121-3129
    • (2005) J Dairy Sci , vol.88 , pp. 3121-3129
    • Lehmann, L.1    Buckin, V.2
  • 49
    • 1842332172 scopus 로고    scopus 로고
    • Rheological properties at small (Dynamic) and large (yield) deformations of acid gels made from heated milk
    • Lucey, J. A., Teo, C. T., Munro, P. A., & Singh, H. (1997). Rheological properties at small (dynamic) and large (yield) deformations of acid gels made from heated milk. Journal of Dairy Research, 64(04), 591-600
    • (1997) Journal of Dairy Research , vol.64 , Issue.4 , pp. 591-600
    • Lucey, J.A.1    Teo, C.T.2    Munro, P.A.3    Singh, H.4
  • 50
    • 1642394974 scopus 로고    scopus 로고
    • Milk ph as a function of co2 concentration, temperature, and pressure in a heat exchanger
    • Ma Y, Barbano DM (2003) Milk pH as a function of CO2 concentration, temperature, and pressure in a heat exchanger. J Dairy Sci 86:3822-3830
    • (2003) J Dairy Sci , vol.86 , pp. 3822-3830
    • Ma, Y.1    Barbano, D.M.2
  • 51
    • 0032817454 scopus 로고    scopus 로고
    • Heat stability of milk emulsions: Phospholipid-protein interactions
    • McCrae CH (1999) Heat stability of milk emulsions: phospholipid-protein interactions. Int Dairy J 9:227-231
    • (1999) Int Dairy J , vol.9 , pp. 227-231
    • Mc Crae, C.H.1
  • 53
    • 0343305377 scopus 로고
    • Effect of formaldehyde on heat stability of milk
    • Metwalli AAM, Van Boekel MAJS (1995) Effect of formaldehyde on heat stability of milk. Neth Milk Dairy J 49:177-189
    • (1995) Neth Milk Dairy J , vol.49 , pp. 177-189
    • Metwalli, A.1    Van Boekel, M.2
  • 54
    • 0342516715 scopus 로고    scopus 로고
    • Effect of urea on heat coagulation of milk
    • Metwalli AAM, van Boekel MAJS (1996) Effect of urea on heat coagulation of milk. Neth Milk Dairy J 50:459-476
    • (1996) Neth Milk Dairy J , vol.50 , pp. 459-476
    • Metwalli, A.1    Van Boekel, M.2
  • 56
    • 85010246495 scopus 로고
    • The coagulation temperature of milk as affected by ph, salts, evaporation and previous heat treatment
    • Miller PG, Sommer HH (1940) The coagulation temperature of milk as affected by pH, salts, evaporation and previous heat treatment. J Dairy Sci 23:405-421
    • (1940) J Dairy Sci , vol.23 , pp. 405-421
    • Miller, P.G.1    Sommer, H.H.2
  • 57
    • 36749039096 scopus 로고
    • Some organic acids in raw and heated milk
    • Morr CV, Harper NJ, Gould IA (1957) Some organic acids in raw and heated milk. J Dairy Sci 40:964-972
    • (1957) J Dairy Sci , vol.40 , pp. 964-972
    • Morr, C.V.1    Harper, N.J.2    Gould, I.A.3
  • 58
    • 25144525228 scopus 로고    scopus 로고
    • Influence of transglutaminase treatment on properties of micel- lar casein and products made therefrom
    • Mounsey JS, OKennedy BT, Kelly PM (2005) Influence of transglutaminase treatment on properties of micel- lar casein and products made therefrom. Lait 85:405-418
    • (2005) Lait , vol.85 , pp. 405-418
    • Mounsey, J.S.1    O Kennedy, B.T.2    Kelly, P.M.3
  • 59
    • 84972054408 scopus 로고
    • Effect of urea on the heat coagulation of the caseinate complex in skim- milk
    • Muir DD, Sweetsur AWM (1977) Effect of urea on the heat coagulation of the caseinate complex in skim- milk. J Dairy Res 44:249-257
    • (1977) J Dairy Res , vol.44 , pp. 249-257
    • Muir, D.D.1    Sweetsur, A.2
  • 60
    • 85010248800 scopus 로고
    • The effects of formaldehyde and copper salts on the heat stability of evaporated milk
    • Nelson V (1954) The effects of formaldehyde and copper salts on the heat stability of evaporated milk. J Dairy Sci 37:825-829
    • (1954) J Dairy Sci , vol.37 , pp. 825-829
    • Nelson, V.1
  • 61
    • 0011298388 scopus 로고
    • Effect of protein and salt concentrations on the heat stability of evaporated milk
    • Newstead DF (1977) Effect of protein and salt concentrations on the heat stability of evaporated milk. NZ J Dairy Sci Technol 12:171-175
    • (1977) NZ J Dairy Sci Technol , vol.12 , pp. 171-175
    • Newstead, D.F.1
  • 63
    • 0742331980 scopus 로고    scopus 로고
    • Heat-induced coagulation of milk
    • Fox PF, McSweeney PLH, 3rd edn, Proteins. Kluwer Academic/Plenum, New York
    • OConnell JE, Fox PF (2003) Heat-induced coagulation of milk. In: Fox PF, McSweeney PLH (eds) Advanced dairy chemistry, vol 1, 3rd edn, Proteins. Kluwer Academic/Plenum, New York, pp 879-945
    • (2003) Advanced Dairy Chemistry , vol.1 , pp. 879-945
    • O Connell, J.E.1    Fox, P.F.2
  • 64
    • 0032047305 scopus 로고    scopus 로고
    • Kinetics of denaturation and aggregation of whey proteins in skim milk heated in an ultra-high temperature (Uht) pilot plant
    • Oldfield DJ, Singh H, Taylor MW, Pearce KN (1998a) Kinetics of denaturation and aggregation of whey proteins in skim milk heated in an ultra-high temperature (UHT) pilot plant. Int Dairy J 8:311-318
    • (1998) Int Dairy J , vol.8 , pp. 311-318
    • Oldfield, D.J.1    Singh, H.2    Taylor, M.W.3    Pearce, K.N.4
  • 65
    • 0032172447 scopus 로고    scopus 로고
    • Association of p-lactoglobulin and a-lactalbumin with the casein micelles in skim milk heated in an ultra-high temperature plant
    • Oldfield DJ, Singh H, Taylor MW (1998b) Association of P-lactoglobulin and a-lactalbumin with the casein micelles in skim milk heated in an ultra-high temperature plant. Int Dairy J 8:765-770
    • (1998) Int Dairy J , vol.8 , pp. 765-770
    • Oldfield, D.J.1    Singh, H.2    Taylor, M.W.3
  • 66
    • 77949286588 scopus 로고    scopus 로고
    • Measurement of ionic calcium, ph, and soluble divalent cations in milk at high temperature
    • On-Nom N, Grandison AS, Lewis MJ (2010) Measurement of ionic calcium, pH, and soluble divalent cations in milk at high temperature. J Dairy Sci 93:515-523
    • (2010) J Dairy Sci , vol.93 , pp. 515-523
    • On-Nom, N.1    Grandison, A.S.2    Lewis, M.J.3
  • 67
    • 0000873734 scopus 로고
    • The membranes of recombined fat globules in milk 2. Composition
    • Oortwijn H, Walstra P (1979) The membranes of recombined fat globules in milk 2. Composition. Neth Milk Dairy J 33:134-154
    • (1979) Neth Milk Dairy J , vol.33 , pp. 134-154
    • Oortwijn, H.1    Walstra, P.2
  • 69
    • 0036365981 scopus 로고    scopus 로고
    • Effect of transglutaminase on the heat stability of milk: A possible mechanism
    • OSullivan MM, Kelly AL, Fox PF (2002) Effect of transglutaminase on the heat stability of milk: a possible mechanism. J Dairy Sci 85:1-7
    • (2002) J Dairy Sci , vol.85 , pp. 1-7
    • O Sullivan, M.M.1    Kelly, A.L.2    Fox, P.F.3
  • 70
    • 84971790175 scopus 로고
    • Observations on the heat-induced salt balance changes in milk. I. Effect of heating time between 4 and 90°c
    • Pouliot Y, Boulet M, Paquin P (1989) Observations on the heat-induced salt balance changes in milk. I. Effect of heating time between 4 and 90°C. J Dairy Res 56: 185-192
    • (1989) J Dairy Res , vol.56 , pp. 185-192
    • Pouliot, Y.1    Boulet, M.2    Paquin, P.3
  • 71
    • 0001319313 scopus 로고
    • The heat coagulation of milk. Ii. Variations in sensitivity of casein to calcium ions
    • Pyne GT (1958) The heat coagulation of milk. II. Variations in sensitivity of casein to calcium ions. J Dairy Res 25:467-474
    • (1958) J Dairy Res , vol.25 , pp. 467-474
    • Pyne, G.T.1
  • 72
    • 0001175301 scopus 로고
    • Factors affecting the heat stability of milk
    • Rose D (1962) Factors affecting the heat stability of milk. J Dairy Sci 45:1305-1311
    • (1962) J Dairy Sci , vol.45 , pp. 1305-1311
    • Rose, D.1
  • 73
    • 0011446218 scopus 로고
    • Heat stability of milk: A review
    • Rose D (1963) Heat stability of milk: a review. Dairy Sci Abstracts 25:45-52
    • (1963) Dairy Sci Abstracts , vol.25 , pp. 45-52
    • Rose, D.1
  • 74
    • 0011342434 scopus 로고
    • Composition of ultrafiltrates from milk heated at 80 to 230° f
    • relation to heat stability
    • Rose D, Tessier H (1959) Composition of ultrafiltrates from milk heated at 80 to 230° F. In relation to heat stability. J Dairy Sci 42:969-980
    • (1959) J Dairy Sci , vol.42 , pp. 969-980
    • Rose, D.1    Tessier, H.2
  • 75
    • 84974224124 scopus 로고
    • Heat stability of milk: Synergic action of urea and carbonyl compounds
    • Shalabi SI, Fox PF (1982a) Heat stability of milk: synergic action of urea and carbonyl compounds. J Dairy Res 49:197-207
    • (1982) J Dairy Res , vol.49 , pp. 197-207
    • Shalabi, S.I.1    Fox, P.F.2
  • 76
    • 0020212652 scopus 로고
    • Heat stability of milk: Influence of modification of lysine and arginine on the heat stability-ph profile
    • Shalabi SI, Fox PF (1982b) Heat stability of milk: influence of modification of lysine and arginine on the heat stability-pH profile. J Dairy Res 49:607-617
    • (1982) J Dairy Res , vol.49 , pp. 607-617
    • Shalabi, S.I.1    Fox, P.F.2
  • 77
    • 0001770281 scopus 로고
    • Heat-induced changes in caseins including interactions with whey proteins
    • Fox PF, International Dairy Federation, Brussels
    • Singh H (1995) Heat-induced changes in caseins including interactions with whey proteins. In: Fox PF (ed) Heat-induced changes in milk. International Dairy Federation, Brussels, pp 86-99
    • (1995) Heat-Induced Changes in Milk , pp. 86-99
    • Singh, H.1
  • 78
    • 2442688971 scopus 로고    scopus 로고
    • Heat stability of milk
    • Singh H (2004) Heat stability of milk. Int J Dairy Technol 57:111-119
    • (2004) Int J Dairy Technol , vol.57 , pp. 111-119
    • Singh, H.1
  • 79
    • 84985200254 scopus 로고
    • Aggregation and dissociation of milk protein complexes in heated reconstituted concentrated skim milks
    • Singh H, Creamer LK (1991a) Aggregation and dissociation of milk protein complexes in heated reconstituted concentrated skim milks. J Food Sci 56:238-246
    • (1991) J Food Sci , vol.56 , pp. 238-246
    • Singh, H.1    Creamer, L.K.2
  • 80
    • 84974200389 scopus 로고
    • Influence of concentration of milk solids on the dissociation of micellar k-casein on heating reconstituted milk at 120°c
    • Singh H, Creamer LK (1991b) Influence of concentration of milk solids on the dissociation of micellar K-casein on heating reconstituted milk at 120°C. J Dairy Res 58:99-105
    • (1991) J Dairy Res , vol.58 , pp. 99-105
    • Singh, H.1    Creamer, L.K.2
  • 81
    • 84974486877 scopus 로고
    • Denaturation, aggregation and heat stability of milk protein during the manufacture of skim milk powder
    • Singh H, Creamer LK (1991c) Denaturation, aggregation and heat stability of milk protein during the manufacture of skim milk powder. J Dairy Res 58:269-283
    • (1991) J Dairy Res , vol.58 , pp. 269-283
    • Singh, H.1    Creamer, L.K.2
  • 82
    • 0001353383 scopus 로고
    • Heat stability of milk
    • Fox PF, 2nd edn, Proteins, London
    • Singh H, Creamer LK (1992) Heat stability of milk. In: Fox PF (ed) Advanced dairy chemistry, vol 1, 2nd edn, Proteins. Elsevier Applied Science, London, pp 621-656
    • (1992) Elsevier Applied Science , vol.1 , pp. 621-656
    • Singh, H.1    Creamer, L.K.2
  • 83
    • 0001876853 scopus 로고
    • Heat stability of milk: Ph- dependent dissociation of micellar k-casein on heating milk at ultra high temperatures
    • Singh H, Fox PF (1985a) Heat stability of milk: pH- dependent dissociation of micellar K-casein on heating milk at ultra high temperatures. J Dairy Res 52: 529-538
    • (1985) J Dairy Res , vol.52 , pp. 529-538
    • Singh, H.1    Fox, P.F.2
  • 84
    • 84974220768 scopus 로고
    • Heat stability of milk: The mechanism of stabilization by formaldehyde
    • Singh H, Fox PF (1985b) Heat stability of milk: the mechanism of stabilization by formaldehyde. J Dairy Res 52:65-76
    • (1985) J Dairy Res , vol.52 , pp. 65-76
    • Singh, H.1    Fox, P.F.2
  • 85
    • 0000090641 scopus 로고
    • Heat stability of milk: Further studies on the ph-dependent dissociation of micellar k-casein
    • Singh H, Fox PF (1986) Heat stability of milk: further studies on the pH-dependent dissociation of micellar K-casein. J Dairy Res 53:237-248
    • (1986) J Dairy Res , vol.53 , pp. 237-248
    • Singh, H.1    Fox, P.F.2
  • 86
    • 84974189071 scopus 로고
    • Heat stability of milk: Influence of modifying sulphydryl-disulphide interactions on the heat coagulation time-ph profile
    • Singh H, Fox PF (1987a) Heat stability of milk: influence of modifying sulphydryl-disulphide interactions on the heat coagulation time-pH profile. J Dairy Res 54:347-359
    • (1987) J Dairy Res , vol.54 , pp. 347-359
    • Singh, H.1    Fox, P.F.2
  • 87
    • 84974081031 scopus 로고
    • Heat stability of milk: Role of p-lactoglobulin in the ph-dependent dissociation of micellar k-casein
    • Singh H, Fox PF (1987b) Heat stability of milk: role of p-lactoglobulin in the pH-dependent dissociation of micellar K-casein. J Dairy Res 54:509-521
    • (1987) J Dairy Res , vol.54 , pp. 509-521
    • Singh, H.1    Fox, P.F.2
  • 88
    • 84974126370 scopus 로고
    • Heat stability of milk: Influence of colloidal and soluble salts and protein modification on the ph-dependent dissociation of micellar k-casein
    • Singh H, Fox PF (1987c) Heat stability of milk: influence of colloidal and soluble salts and protein modification on the pH-dependent dissociation of micellar K-casein. J Dairy Res 54:523-534
    • (1987) J Dairy Res , vol.54 , pp. 523-534
    • Singh, H.1    Fox, P.F.2
  • 89
    • 0011339018 scopus 로고
    • The use of permitted additives and heat-treatment to optimize the heat- stability of skim milk and concentrated skim milk
    • Sweetsur AWM, Muir DD (1980) The use of permitted additives and heat-treatment to optimize the heat- stability of skim milk and concentrated skim milk. J Soc Dairy Technol 33:101-105
    • (1980) J Soc Dairy Technol , vol.33 , pp. 101-105
    • Sweetsur, A.1    Muir, D.D.2
  • 90
    • 84975997323 scopus 로고
    • Effect of homogenization on the heat stability of milk
    • Sweetsur AM, Muir DD (1983a) Effect of homogenization on the heat stability of milk. J Dairy Res 50:291-300
    • (1983) J Dairy Res , vol.50 , pp. 291-300
    • Sweetsur, A.M.1    Muir, D.D.2
  • 91
    • 84974324460 scopus 로고
    • Influence of sulphy- dryl group interactions on the heat stability ofhomogenized concentrated milk
    • Sweetsur AM, Muir DD (1983b) Influence of sulphy- dryl group interactions on the heat stability ofhomogenized concentrated milk. J Dairy Res 50: 301-308
    • (1983) J Dairy Res , vol.50 , pp. 301-308
    • Sweetsur, A.M.1    Muir, D.D.2
  • 93
    • 0032817307 scopus 로고    scopus 로고
    • Effect of various preheat treatments on the heat stability of unconcentrated milk
    • Tan-Kintia RH, Fox PF (1999) Effect of various preheat treatments on the heat stability of unconcentrated milk. Int Dairy J 9:219-225
    • (1999) Int Dairy J , vol.9 , pp. 219-225
    • Tan-Kintia, R.H.1    Fox, P.F.2
  • 96
    • 0043241649 scopus 로고    scopus 로고
    • Casein-whey protein interactions in heated milk: The influence of ph
    • Vasbinder AJ, de Kruif CG (2003) Casein-whey protein interactions in heated milk: the influence of pH. Int Dairy J 13:669-677
    • (2003) Int Dairy J , vol.13 , pp. 669-677
    • Vasbinder, A.J.1    De Kruif, C.G.2
  • 97
    • 85025797643 scopus 로고
    • On casein micelles
    • Walstra P (1990) On casein micelles. J Dairy Sci 73: 1965-1979
    • (1990) J Dairy Sci , vol.73 , pp. 1965-1979
    • Walstra, P.1
  • 98
    • 0005732017 scopus 로고
    • The stability of milk protein to heat. Iii. Objective measurement of heat stability of milk
    • White JCD, Davies DT (1966) The stability of milk protein to heat. III. Objective measurement of heat stability of milk. J Dairy Res 33:93-102
    • (1966) J Dairy Res , vol.33 , pp. 93-102
    • White, J.1    Davies, D.T.2


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