메뉴 건너뛰기




Volumn 83, Issue 3, 2000, Pages 378-386

The two-stage coagulation of milk proteins in the minimum of the heat coagulation time-pH profile of milk: Effect of casein micelle size

Author keywords

Casein micelle size; Heat stability; Milk

Indexed keywords

CASEIN; MILK PROTEIN;

EID: 0034150548     PISSN: 00220302     EISSN: None     Source Type: Journal    
DOI: 10.3168/jds.S0022-0302(00)74892-2     Document Type: Article
Times cited : (67)

References (38)
  • 1
    • 0000777071 scopus 로고
    • Relation between micelle size and formation of soluble casein on heating concentrated milk
    • Aoki, T., and Y. Kako. 1983. Relation between micelle size and formation of soluble casein on heating concentrated milk. J. Dairy Res. 50:207-213.
    • (1983) J. Dairy Res. , vol.50 , pp. 207-213
    • Aoki, T.1    Kako, Y.2
  • 2
    • 0000145787 scopus 로고
    • Formation of soluble casein in whey protein-free milk heated at high temperature
    • Aoki, T., H. Suzuki, and T. Imamura. 1974. Formation of soluble casein in whey protein-free milk heated at high temperature. Milchwissenschaft 29:589-594.
    • (1974) Milchwissenschaft , vol.29 , pp. 589-594
    • Aoki, T.1    Suzuki, H.2    Imamura, T.3
  • 3
    • 0000131192 scopus 로고
    • A spectrofluorimetric approach to the estimation of the surface hydrophobicity modifications in milk proteins upon thermal treatment
    • Bonomi, F., S. Iametti, E. Pagliarini, and C. Peri. 1988. A spectrofluorimetric approach to the estimation of the surface hydrophobicity modifications in milk proteins upon thermal treatment. Milchwissenschaft 43:281-285.
    • (1988) Milchwissenschaft , vol.43 , pp. 281-285
    • Bonomi, F.1    Iametti, S.2    Pagliarini, E.3    Peri, C.4
  • 4
    • 0015828962 scopus 로고
    • The distribution of glyco-κ-casein and carbohydrate-free κ-casein between large and small bovine casein micelles and its implication in casein micelle structure
    • Creamer, L. K., J. V. Wheelock, and D. Samuel. 1973. The distribution of glyco-κ-casein and carbohydrate-free κ-casein between large and small bovine casein micelles and its implication in casein micelle structure. Biochim. Biophys. Acta 317:202-206.
    • (1973) Biochim. Biophys. Acta , vol.317 , pp. 202-206
    • Creamer, L.K.1    Wheelock, J.V.2    Samuel, D.3
  • 5
    • 84972090718 scopus 로고
    • Heat stability of milk
    • Darling, D. F. 1980. Heat stability of milk. J. Dairy Res. 47:199-210.
    • (1980) J. Dairy Res. , vol.47 , pp. 199-210
    • Darling, D.F.1
  • 6
    • 84974315624 scopus 로고
    • Electrophoretic mobility of casein micellles
    • Darling, D. F., and J. Dickson. 1979. Electrophoretic mobility of casein micellles. J. Dairy Res. 46:441-451.
    • (1979) J. Dairy Res. , vol.46 , pp. 441-451
    • Darling, D.F.1    Dickson, J.2
  • 7
    • 84974325077 scopus 로고
    • Variation in protein composition of bovine casein micelles and serum casein in relation to casein micelle size and milk temperature
    • Davies, D. T., and A.J.R. Law. 1983. Variation in protein composition of bovine casein micelles and serum casein in relation to casein micelle size and milk temperature. J. Dairy Res. 50:67-75.
    • (1983) J. Dairy Res. , vol.50 , pp. 67-75
    • Davies, D.T.1    Law, A.J.R.2
  • 8
    • 0002749539 scopus 로고
    • The stability of milk protein to heat: 1. Subjective measurement of heat stability of milk
    • Davies, D. T., and J.C.D. White. 1966. The stability of milk protein to heat: 1. 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.C.D.2
  • 9
    • 0013553113 scopus 로고
    • Participation of hydrophobic bond in complex formation between κ-casein and 3-lactoglobulin
    • Doi, H., S. Ideno, F. Ibuki, and M. Kanamori 1983. Participation of hydrophobic bond in complex formation between κ-casein and 3-lactoglobulin. Agric. Biol. Chem. 47:407-409.
    • (1983) Agric. Biol. Chem. , vol.47 , pp. 407-409
    • Doi, H.1    Ideno, S.2    Ibuki, F.3    Kanamori, M.4
  • 10
    • 0002266872 scopus 로고
    • Heat-induced coagulation of milk
    • P. F. Fox, ed. Applied Science Publishers, London, United Kingdom
    • Fox, P. F. 1982. Heat-induced coagulation of milk. Pages 189-228 in Developments in Dairy Chemistry - 1 Proteins. P. F. Fox, ed. Applied Science Publishers, London, United Kingdom.
    • (1982) Developments in Dairy Chemistry - 1 Proteins , pp. 189-228
    • Fox, P.F.1
  • 11
    • 0003089568 scopus 로고
    • Effect of heating at 200°C on casein micelles in milk: A metal shadowing and negative staining electron microscope study
    • Harwalkar, V. R., P. Allan-Wojtas, and M. Kalab. 1989. Effect of heating at 200°C on casein micelles in milk: A metal shadowing and negative staining electron microscope study. Food Microstruct. 8:217-224.
    • (1989) Food Microstruct. , vol.8 , pp. 217-224
    • Harwalkar, V.R.1    Allan-Wojtas, P.2    Kalab, M.3
  • 12
    • 0000930823 scopus 로고
    • Separation of major casein fractions using cation-exchange fast liquid chromatography
    • Hollar, C. M., A.J.R. Law, D. G. Dalgleish, and R. J. Brown. 1991. Separation of major casein fractions using cation-exchange fast liquid chromatography. J. Dairy Sci. 74:2403-2409.
    • (1991) J. Dairy Sci. , vol.74 , pp. 2403-2409
    • Hollar, C.M.1    Law, A.J.R.2    Dalgleish, D.G.3    Brown, R.J.4
  • 13
    • 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
  • 14
    • 0001871181 scopus 로고    scopus 로고
    • The hairy casein micelle: Evolution of the concept and its implications for dairy technology
    • Holt, C., and D. S. Horne. 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
  • 15
    • 0000547124 scopus 로고
    • Preparation and properties of a salt solution which simulates milk ultrafiltrate
    • Jenness, R., and J. Koops. 1962. Preparation and properties of a salt solution which simulates milk ultrafiltrate. Neth. Milk Dairy J. 16:153-164.
    • (1962) Neth. Milk Dairy J. , vol.16 , pp. 153-164
    • Jenness, R.1    Koops, J.2
  • 16
    • 0001313867 scopus 로고
    • The heat stability of milk: Formation of soluble proteins and protein depleted micelles at elevated temperatures
    • Kudo, S. 1980. The heat stability of milk: formation of soluble proteins and protein depleted micelles at elevated temperatures. N.Z. J. Dairy Sci. Technol. 15:255-263.
    • (1980) N.Z. J. Dairy Sci. Technol. , vol.15 , pp. 255-263
    • Kudo, S.1
  • 17
    • 0030522273 scopus 로고    scopus 로고
    • The influence of genetic variants of milk proteins on the compositional and technological properties of milk 1: Casein micelle size and the content of non-glycosylated κ-casein
    • Lodes, A., I. Krause, J. Buchberger, J. Aumann, and H. Klostermeyer. 1996. The influence of genetic variants of milk proteins on the compositional and technological properties of milk 1: Casein micelle size and the content of non-glycosylated κ-casein. Milchwissenschaft 51:368-373.
    • (1996) Milchwissenschaft , vol.51 , pp. 368-373
    • Lodes, A.1    Krause, I.2    Buchberger, J.3    Aumann, J.4    Klostermeyer, H.5
  • 20
    • 0018461763 scopus 로고
    • Developments in column chromatography for separation of casein micelles
    • McGann, T.C.A., R. D. Kearney, and W. J. Donnelly. 1979. Developments in column chromatography for separation of casein micelles. J. Dairy Res. 46:307-311.
    • (1979) J. Dairy Res. , vol.46 , pp. 307-311
    • McGann, T.C.A.1    Kearney, R.D.2    Donnelly, W.J.3
  • 21
    • 85010246495 scopus 로고
    • The coagulation temperature of milk as affected by pH, salts, evaporation and previous heat treatment
    • Miller, P. G., and H. H. Sommer. 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
  • 22
    • 0032147679 scopus 로고    scopus 로고
    • Effect of tea, coffee and cocoa extracts on the colloidal stability of milk and concentrated milk
    • O'Connell, J. E., P. D. Fox, R. Tan-Kintia, and P. F. Fox. 1998. Effect of tea, coffee and cocoa extracts on the colloidal stability of milk and concentrated milk. Int. Dairy J. 8:689-693.
    • (1998) Int. Dairy J. , vol.8 , pp. 689-693
    • O'Connell, J.E.1    Fox, P.D.2    Tan-Kintia, R.3    Fox, P.F.4
  • 23
    • 84971897381 scopus 로고
    • Theory for the heat-induced coagulation of a type A milk
    • Parker, T. G., D. S. Horne, and D. G. Dalgleish. 1979. Theory for the heat-induced coagulation of a type A milk. J. Dairy Res. 46:377-380.
    • (1979) J. Dairy Res. , vol.46 , pp. 377-380
    • Parker, T.G.1    Horne, D.S.2    Dalgleish, D.G.3
  • 24
    • 0042698143 scopus 로고
    • Factors affecting the pH sensitivity of the heat stability of milk from individual cows
    • Rose, D. 1961. Factors affecting the pH sensitivity of the heat stability of milk from individual cows. J. Dairy Sci. 44:1405-1413.
    • (1961) J. Dairy Sci. , vol.44 , pp. 1405-1413
    • Rose, D.1
  • 25
    • 0039022189 scopus 로고
    • Factors affecting the pH sensitivity of the heat stability of evaporated milk
    • Rose, D. 1961. Factors affecting the pH sensitivity of the heat stability of evaporated milk. J. Dairy Sci. 44:1763-1772.
    • (1961) J. Dairy Sci. , vol.44 , pp. 1763-1772
    • Rose, D.1
  • 26
    • 0000303371 scopus 로고
    • Protein stability problems
    • Rose, D. 1965. Protein stability problems. J. Dairy Sci. 48:139-146.
    • (1965) J. Dairy Sci. , vol.48 , pp. 139-146
    • Rose, D.1
  • 27
    • 0013950348 scopus 로고
    • Appearance and size of micelles from bovine milk
    • Rose, D., and J. R. Colvin. 1966. Appearance and size of micelles from bovine milk. J. Dairy Sci. 49:1091-1097.
    • (1966) J. Dairy Sci. , vol.49 , pp. 1091-1097
    • Rose, D.1    Colvin, J.R.2
  • 28
    • 0001776309 scopus 로고
    • Colloidal aspects of casein
    • Schmidt, D. G. 1980. Colloidal aspects of casein. Neth. Milk Dairy J. 34:42-64.
    • (1980) Neth. Milk Dairy J. , vol.34 , pp. 42-64
    • Schmidt, D.G.1
  • 29
    • 0002429127 scopus 로고
    • Association of caseins and casein micelle structure
    • P. F. Fox, ed. Applied Science Publishers, London, United Kingdom
    • Schmidt, D. G. 1982. Association of caseins and casein micelle structure. Pages 61-86 in Developments in Dairy Chemistry 1 Proteins. P. F. Fox, ed. Applied Science Publishers, London, United Kingdom.
    • (1982) Developments in Dairy Chemistry 1 Proteins , pp. 61-86
    • Schmidt, D.G.1
  • 30
    • 0001180287 scopus 로고
    • Properties of artificial casein micelles 2. Stability towards ethanol, dialysis, pressure and heat in relation to casein composition
    • Schmidt, D. G., and J. Koops. 1977. Properties of artificial casein micelles 2. Stability towards ethanol, dialysis, pressure and heat in relation to casein composition. Neth. Milk Dairy J. 31:342-357.
    • (1977) Neth. Milk Dairy J. , vol.31 , pp. 342-357
    • Schmidt, D.G.1    Koops, J.2
  • 32
    • 84974081031 scopus 로고
    • Heat stability of milk: Role of β-lactoglobulin in the pH-dependent dissociation of micellar κ-casein
    • Singh, H., and P. F. Fox. 1987. Heat stability of milk: Role of β-lactoglobulin in the pH-dependent dissociation of micellar κ-casein. J. Dairy Res. 54:509-521.
    • (1987) J. Dairy Res. , vol.54 , pp. 509-521
    • Singh, H.1    Fox, P.F.2
  • 33
    • 0015902350 scopus 로고
    • A model for the formation and structure of casein micelles from subunits of variable composition
    • Slattery, C. W., and R. Evard. 1973. A model for the formation and structure of casein micelles from subunits of variable composition. Biochim. Biophys. Acta 317:529-538.
    • (1973) Biochim. Biophys. Acta , vol.317 , pp. 529-538
    • Slattery, C.W.1    Evard, R.2
  • 34
    • 84976128099 scopus 로고
    • Studies on the heat stability of milk protein. 1: Interconversion of type A to type B milk heat stability curves
    • Sweetsur, A.W.M., and J.C.D. White. 1974. Studies on the heat stability of milk protein. 1: Interconversion of type A to type B milk heat stability curves. J. Dairy Res. 41:349-358.
    • (1974) J. Dairy Res. , vol.41 , pp. 349-358
    • Sweetsur, A.W.M.1    White, J.C.D.2
  • 35
    • 0032345046 scopus 로고    scopus 로고
    • Microfiltration of milk with ceramic membranes: Influence on casein composition and heat stability
    • Tziboula, A., W. Steele, I. West, and D. D. Muir. 1998. Microfiltration of milk with ceramic membranes: Influence on casein composition and heat stability. Milchwissenschaft 53:8-11.
    • (1998) Milchwissenschaft , vol.53 , pp. 8-11
    • Tziboula, A.1    Steele, W.2    West, I.3    Muir, D.D.4
  • 37
    • 0008128130 scopus 로고
    • The thiobarbituric acid assay of sialic acid
    • Warren, L. 1959. The thiobarbituric acid assay of sialic acid. J. Biol. Chem. 234:1971-1975.
    • (1959) J. Biol. Chem. , vol.234 , pp. 1971-1975
    • Warren, L.1
  • 38
    • 0011153076 scopus 로고
    • The influence of casein micelle size on selected functional properties of bulk milk proteins
    • Zbikowska, A., J. Dziuda, H. Jaworska, and A. Zaborniak. 1992. The influence of casein micelle size on selected functional properties of bulk milk proteins. Polish J. Food Nutr. Sci. 42:21-32.
    • (1992) Polish J. Food Nutr. Sci. , vol.42 , pp. 21-32
    • Zbikowska, A.1    Dziuda, J.2    Jaworska, H.3    Zaborniak, A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.