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Volumn 1, Issue C, 2004, Pages 47-70

Rennet-induced Coagulation of Milk

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EID: 34247638642     PISSN: 1874558X     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S1874-558X(04)80062-9     Document Type: Chapter
Times cited : (78)

References (178)
  • 2
    • 0039016084 scopus 로고    scopus 로고
    • Influence of pH on the effects of high pressure on milk proteins
    • Arias M., Lopez-Fandino R., and Olano A. Influence of pH on the effects of high pressure on milk proteins. Milchwissenschaft 53 (2000) 191-194
    • (2000) Milchwissenschaft , vol.53 , pp. 191-194
    • Arias, M.1    Lopez-Fandino, R.2    Olano, A.3
  • 3
    • 85005681568 scopus 로고
    • Elimination of the development of bitter flavour in Cheddar cheese made from milk containing heatdenatured whey protein
    • Banks J.M. Elimination of the development of bitter flavour in Cheddar cheese made from milk containing heatdenatured whey protein. J. Soc. Dairy Technol. 41 (1988) 37-41
    • (1988) J. Soc. Dairy Technol. , vol.41 , pp. 37-41
    • Banks, J.M.1
  • 4
    • 77957106220 scopus 로고
    • Yield and quality of Cheddar cheese produced using a fermentation-derived calf chymosin
    • Banks J.M. Yield and quality of Cheddar cheese produced using a fermentation-derived calf chymosin. Milchwissenschaft 40 (1992) 209-212
    • (1992) Milchwissenschaft , vol.40 , pp. 209-212
    • Banks, J.M.1
  • 5
    • 0000938026 scopus 로고
    • Increasing the yield of Cheddar cheese by acidification of milk containing heat denatured whey protein
    • Banks J.M., Stewart G., Muir D.D., and West I.G. Increasing the yield of Cheddar cheese by acidification of milk containing heat denatured whey protein. Milchwissenschaft 42 (1987) 212-215
    • (1987) Milchwissenschaft , vol.42 , pp. 212-215
    • Banks, J.M.1    Stewart, G.2    Muir, D.D.3    West, I.G.4
  • 7
    • 0000452025 scopus 로고
    • The structure of casein aggregates during renneting studied by indirect Fourier transformation and inverse Laplace transformation of static and dynamic light scattering data, respectively
    • Bauer R., Hansen M., Hansen S., Øgendal L., Lomholt S., Qvist K., and Home D. The structure of casein aggregates during renneting studied by indirect Fourier transformation and inverse Laplace transformation of static and dynamic light scattering data, respectively. J. Chem. Phys. 103 (1995) 2725-2737
    • (1995) J. Chem. Phys. , vol.103 , pp. 2725-2737
    • Bauer, R.1    Hansen, M.2    Hansen, S.3    Øgendal, L.4    Lomholt, S.5    Qvist, K.6    Home, D.7
  • 9
    • 55749107160 scopus 로고
    • Viscoelastic properties of coagulating milk
    • Bohlin L., Hegg P., and Ljusberg-Wahren H. Viscoelastic properties of coagulating milk. J. Dairy Sci. 67 (1984) 729-734
    • (1984) J. Dairy Sci. , vol.67 , pp. 729-734
    • Bohlin, L.1    Hegg, P.2    Ljusberg-Wahren, H.3
  • 10
    • 0003426521 scopus 로고
    • Fractal Aggregates in Relation to Formation and Properties of Particle Gels
    • Wageningen, The Netherlands.
    • Wageningen, The Netherlands. Bremer L.B.G. Fractal Aggregates in Relation to Formation and Properties of Particle Gels. PhD Thesis, Wageningen Agricultural University (1992)
    • (1992) PhD Thesis, Wageningen Agricultural University
    • Bremer, L.B.G.1
  • 11
    • 0000521011 scopus 로고
    • Theoretical and experimental study of the fractal nature of the structure of casein gels
    • Bremer L.B.G., Van Vliet T., and Walstra P. Theoretical and experimental study of the fractal nature of the structure of casein gels. J. Chem. Soc. Faraday Trans. 185 (1989) 3359-3372
    • (1989) J. Chem. Soc. Faraday Trans. , vol.185 , pp. 3359-3372
    • Bremer, L.B.G.1    Van Vliet, T.2    Walstra, P.3
  • 12
    • 0040621267 scopus 로고
    • The influence of temperature on the flocculation of renneted casein micelles
    • Brinkhuis J., and Payens T.A.J. The influence of temperature on the flocculation of renneted casein micelles. Biophys. Chem. 19 (1984) 75-81
    • (1984) Biophys. Chem. , vol.19 , pp. 75-81
    • Brinkhuis, J.1    Payens, T.A.J.2
  • 13
    • 0004195116 scopus 로고
    • The Structure and Physical Properties of Flocculating Colloids
    • Cambridge, UK.
    • Cambridge, UK. Brown W.D. The Structure and Physical Properties of Flocculating Colloids. PhD Thesis, University of Cambridge (1987)
    • (1987) PhD Thesis, University of Cambridge
    • Brown, W.D.1
  • 15
    • 0023644732 scopus 로고
    • Kinetics of milk coagulation. III. Mathematical modelling of the kinetics of curd formation following enzymatic hydrolysis of κ-casein - parameter estimation
    • Carlson A., Hill Jr. C.G., and Olson N.F. Kinetics of milk coagulation. III. Mathematical modelling of the kinetics of curd formation following enzymatic hydrolysis of κ-casein - parameter estimation. Biotechnol. Bioeng. 29 (1987) 601-611
    • (1987) Biotechnol. Bioeng. , vol.29 , pp. 601-611
    • Carlson, A.1    Hill Jr., C.G.2    Olson, N.F.3
  • 16
    • 0023644735 scopus 로고
    • Kinetics of milk coagulation. IV The kinetics of the gel-firming process
    • Carlson A., Hill Jr. C.G., and Olson N.F. Kinetics of milk coagulation. IV The kinetics of the gel-firming process. Biotechnol. Bioeng. 29 (1987) 612-624
    • (1987) Biotechnol. Bioeng. , vol.29 , pp. 612-624
    • Carlson, A.1    Hill Jr., C.G.2    Olson, N.F.3
  • 17
    • 84971896253 scopus 로고
    • Determination of the proportion of κ-casein hydrolyzed by rennet on coagulation of skim-milk
    • Chaplin B., and Green M.L. Determination of the proportion of κ-casein hydrolyzed by rennet on coagulation of skim-milk. J. Dairy Res. 47 (1980) 351-358
    • (1980) J. Dairy Res. , vol.47 , pp. 351-358
    • Chaplin, B.1    Green, M.L.2
  • 18
    • 0032054231 scopus 로고    scopus 로고
    • Chymosin and aspartic proteinases
    • Chitpinityol S., and Crabbe M.J.C. Chymosin and aspartic proteinases. Food Chem. 61 (1998) 395-418
    • (1998) Food Chem. , vol.61 , pp. 395-418
    • Chitpinityol, S.1    Crabbe, M.J.C.2
  • 19
    • 77957107312 scopus 로고    scopus 로고
    • The formation and properties of biopolymer gels
    • Dickinson E., and Van Vliet T. (Eds), Royal Society of Chemistry, Brussels
    • Clark A.H., and Amici E.H. The formation and properties of biopolymer gels. In: Dickinson E., and Van Vliet T. (Eds). Food Colloids and Materials (2003), Royal Society of Chemistry, Brussels 35-48
    • (2003) Food Colloids and Materials , pp. 35-48
    • Clark, A.H.1    Amici, E.H.2
  • 20
    • 84974327486 scopus 로고
    • Proteolysis and aggregation of casein micelles treated with immobilized or soluble chymosin
    • Dalgleish D.G. Proteolysis and aggregation of casein micelles treated with immobilized or soluble chymosin. J. Dairy Res. 46 (1979) 653-661
    • (1979) J. Dairy Res. , vol.46 , pp. 653-661
    • Dalgleish, D.G.1
  • 21
    • 84972047808 scopus 로고
    • Effect of milk concentration on rennet coagulation time
    • Dalgleish D.G. Effect of milk concentration on rennet coagulation time. J. Dairy Res. 47 (1980) 231-235
    • (1980) J. Dairy Res. , vol.47 , pp. 231-235
    • Dalgleish, D.G.1
  • 22
    • 0019002111 scopus 로고
    • A mechanism for the chymosin-induced flocculation of casein micelles
    • Dalgleish D.G. A mechanism for the chymosin-induced flocculation of casein micelles. Biophys. Chem. 11 (1980) 147-155
    • (1980) Biophys. Chem. , vol.11 , pp. 147-155
    • Dalgleish, D.G.1
  • 23
    • 84974379663 scopus 로고
    • Coagulation of renneted casein micelles: dependence on temperature, calcium ion concentration and ionic strength
    • Dalgleish D.G. Coagulation of renneted casein micelles: dependence on temperature, calcium ion concentration and ionic strength. J. Dairy Res. 50 (1983) 331-340
    • (1983) J. Dairy Res. , vol.50 , pp. 331-340
    • Dalgleish, D.G.1
  • 24
    • 0001400692 scopus 로고
    • Measurement of electrophoretic mobilities and zeta potentials of particles from milk using laser Doppler electrophoresis
    • Dalgleish D.G. Measurement of electrophoretic mobilities and zeta potentials of particles from milk using laser Doppler electrophoresis. J. Dairy Res. 51 (1984) 425-438
    • (1984) J. Dairy Res. , vol.51 , pp. 425-438
    • Dalgleish, D.G.1
  • 25
    • 85032068794 scopus 로고
    • A new calculation of the kinetics of the renneting reaction
    • Dalgleish D.G. A new calculation of the kinetics of the renneting reaction. J. Dairy Res. 55 (1988) 221-228
    • (1988) J. Dairy Res. , vol.55 , pp. 221-228
    • Dalgleish, D.G.1
  • 26
    • 0000356407 scopus 로고
    • The effect of denaturation of β-lactoglobulin on renneting. A quantitative study
    • Dalgleish D.G. The effect of denaturation of β-lactoglobulin on renneting. A quantitative study. Milchwissenschaft 45 (1990) 491-494
    • (1990) Milchwissenschaft , vol.45 , pp. 491-494
    • Dalgleish, D.G.1
  • 27
    • 0000599870 scopus 로고
    • The enzymatic coagulation of milk
    • Fox P.F. (Ed), Elsevier Applied Science, Cambridge
    • Dalgleish D.G. The enzymatic coagulation of milk. In: Fox P.F. (Ed). Advanced Dairy Chemistry: 1. Proteins (1992), Elsevier Applied Science, Cambridge 579-619
    • (1992) Advanced Dairy Chemistry: 1. Proteins , pp. 579-619
    • Dalgleish, D.G.1
  • 29
    • 0024013824 scopus 로고
    • A geometric model to describe the initial aggregation of partially renneted casein micelles
    • Dalgleish D.G., and Holt C. A geometric model to describe the initial aggregation of partially renneted casein micelles. J. Colloid Interf. Sci. 123 (1988) 80-84
    • (1988) J. Colloid Interf. Sci. , vol.123 , pp. 80-84
    • Dalgleish, D.G.1    Holt, C.2
  • 30
    • 84971758074 scopus 로고
    • pH-induced dissociation of bovine casein micelles. 1. Analysis of liberated caseins
    • Dalgleish D.G., and Law A.J.R. pH-induced dissociation of bovine casein micelles. 1. Analysis of liberated caseins. J. Dairy Res. 55 (1988) 529-538
    • (1988) J. Dairy Res. , vol.55 , pp. 529-538
    • Dalgleish, D.G.1    Law, A.J.R.2
  • 31
    • 0019627896 scopus 로고
    • The coagulation of differently sized micelles by rennet
    • Dalgleish D.G., Brinkhuis J., and Payens T.A.J. The coagulation of differently sized micelles by rennet. Fur. J. Biochem. 119 (1981) 257-261
    • (1981) Fur. J. Biochem. , vol.119 , pp. 257-261
    • Dalgleish, D.G.1    Brinkhuis, J.2    Payens, T.A.J.3
  • 32
    • 15144339704 scopus 로고
    • The rate constants for the aggregation of rennet-treated casein micelles
    • Dalgleish D.G., Payens T.A.J., and Brinkhuis J. The rate constants for the aggregation of rennet-treated casein micelles. Neth. Milk Dairy J. 35 (1981) 381-383
    • (1981) Neth. Milk Dairy J. , vol.35 , pp. 381-383
    • Dalgleish, D.G.1    Payens, T.A.J.2    Brinkhuis, J.3
  • 34
    • 0023812807 scopus 로고
    • Structure and mechanism of formation of chymosin C derived from recombinant chymosin A
    • Danley D.E., and Geoghegan K.F. Structure and mechanism of formation of chymosin C derived from recombinant chymosin A. J. Biol. Chem. 263 (1988) 9785-9789
    • (1988) J. Biol. Chem. , vol.263 , pp. 9785-9789
    • Danley, D.E.1    Geoghegan, K.F.2
  • 35
    • 84971994953 scopus 로고
    • The determination of the zeta potential of casein micelles
    • Darling D.F., and Dickson J. The determination of the zeta potential of casein micelles. J. Dairy Res. 46 (1979) 329-332
    • (1979) J. Dairy Res. , vol.46 , pp. 329-332
    • Darling, D.F.1    Dickson, J.2
  • 36
    • 84971960615 scopus 로고
    • Derivation of a mathematical model for the mechanism of casein micelle coagulation by rennet
    • Darling D.F., and Van Hooydonk A.C.M. Derivation of a mathematical model for the mechanism of casein micelle coagulation by rennet. J. Dairy Res. 48 (1981) 189-200
    • (1981) J. Dairy Res. , vol.48 , pp. 189-200
    • Darling, D.F.1    Van Hooydonk, A.C.M.2
  • 37
    • 84971722091 scopus 로고
    • The content and composition of protein in creamery milks in south-west Scotland
    • Davies D.T., and Law A.J.R. The content and composition of protein in creamery milks in south-west Scotland. J. Dairy Res. 47 (1980) 83-90
    • (1980) J. Dairy Res. , vol.47 , pp. 83-90
    • Davies, D.T.1    Law, A.J.R.2
  • 39
    • 0001306594 scopus 로고
    • Dynamic rheology of rennet curd
    • Dejmek P. Dynamic rheology of rennet curd. J. Dairy Sci. 70 (1987) 1325-1330
    • (1987) J. Dairy Sci. , vol.70 , pp. 1325-1330
    • Dejmek, P.1
  • 40
    • 0032839313 scopus 로고    scopus 로고
    • Casein micelle interactions
    • De Kruif C.G. Casein micelle interactions. Int. Dairy J. 9 (1999) 183-188
    • (1999) Int. Dairy J. , vol.9 , pp. 183-188
    • De Kruif, C.G.1
  • 41
    • 0348114294 scopus 로고    scopus 로고
    • Casein micelle structure, functions and interactions
    • Fox P.F., and McSweeney P.L.H. (Eds), Kluwer, Ithaca, New York
    • De Kruif C.G., and Holt C. Casein micelle structure, functions and interactions. In: Fox P.F., and McSweeney P.L.H. (Eds). Advanced Dairy Chemistry. I. Proteins. 3rd edn (2003), Kluwer, Ithaca, New York 233-276
    • (2003) Advanced Dairy Chemistry. I. Proteins. 3rd edn , pp. 233-276
    • De Kruif, C.G.1    Holt, C.2
  • 42
    • 0001443308 scopus 로고
    • The viscosity of milk during the initial stages of renneting
    • De Kruif C.G., Jeurnink T.J.M., and Zoon P. The viscosity of milk during the initial stages of renneting. Neth. Milk Dairy J. 46 (1992) 123-137
    • (1992) Neth. Milk Dairy J. , vol.46 , pp. 123-137
    • De Kruif, C.G.1    Jeurnink, T.J.M.2    Zoon, P.3
  • 43
    • 21844499766 scopus 로고
    • Study of acid and rennet coagulation of high pressurized milk
    • Desobry-Banon S., Richard F., and Hardy J. Study of acid and rennet coagulation of high pressurized milk. J. Dairy Sci. 77 (1994) 3267-3274
    • (1994) J. Dairy Sci. , vol.77 , pp. 3267-3274
    • Desobry-Banon, S.1    Richard, F.2    Hardy, J.3
  • 44
    • 33645994004 scopus 로고    scopus 로고
    • Colloidal aggregation: mechanisms and implications
    • Dickinson E., and Van Vliet T. (Eds), Royal Society of Chemistry, Dordrecht
    • Dickinson E. Colloidal aggregation: mechanisms and implications. In: Dickinson E., and Van Vliet T. (Eds). Food Colloids: Biopolymers and Materials (2003), Royal Society of Chemistry, Dordrecht 68-83
    • (2003) Food Colloids: Biopolymers and Materials , pp. 68-83
    • Dickinson, E.1
  • 46
    • 33748717996 scopus 로고    scopus 로고
    • Self-consistent-field modelling of casein adsorption. Interactions between two protein-coated surfaces
    • Dickinson E., Home D.S., Pinfield V.J., and Leermakers F.A.M. Self-consistent-field modelling of casein adsorption. Interactions between two protein-coated surfaces. J. Chem. Soc. Faraday 93 (1997) 1785-1790
    • (1997) J. Chem. Soc. Faraday , vol.93 , pp. 1785-1790
    • Dickinson, E.1    Home, D.S.2    Pinfield, V.J.3    Leermakers, F.A.M.4
  • 47
    • 84981420830 scopus 로고
    • Rheological analysis of curd formation
    • Douillard R. Rheological analysis of curd formation. J. Texture Studies 4 (1973) 158-165
    • (1973) J. Texture Studies , vol.4 , pp. 158-165
    • Douillard, R.1
  • 48
    • 0024582853 scopus 로고
    • Specificity of milk clotting enzymes towards bovine κ-casein
    • Dronse H.B., and Foltmann B. Specificity of milk clotting enzymes towards bovine κ-casein. Biochim. Biophys. Acta 995 (1989) 221-224
    • (1989) Biochim. Biophys. Acta , vol.995 , pp. 221-224
    • Dronse, H.B.1    Foltmann, B.2
  • 49
    • 0039068114 scopus 로고
    • Cheese yield experiments and proteolysis by milk-clotting enzymes
    • Emmons D.B., Beckett D.C., and Binns M. Cheese yield experiments and proteolysis by milk-clotting enzymes. J. Dairy Sci. 73 (1990) 2028-2043
    • (1990) J. Dairy Sci. , vol.73 , pp. 2028-2043
    • Emmons, D.B.1    Beckett, D.C.2    Binns, M.3
  • 50
    • 0010319048 scopus 로고
    • Milk clotting enzymes. I. Proteolysis during cheesemaking in relation to estimated losses of yield
    • Emmons D.B., Beckett D.C., and Binns M. Milk clotting enzymes. I. Proteolysis during cheesemaking in relation to estimated losses of yield. J. Dairy Sci. 73 (1990) 2007-2015
    • (1990) J. Dairy Sci. , vol.73 , pp. 2007-2015
    • Emmons, D.B.1    Beckett, D.C.2    Binns, M.3
  • 51
    • 0001707841 scopus 로고
    • Biochemical characteristics of the vegetable rennets from the flowers of cardoon: Comparison to calf rennet
    • Esteves C.L., Verissimo P.C., Faro C.J., and Pires E.V. Biochemical characteristics of the vegetable rennets from the flowers of cardoon: Comparison to calf rennet. J. Dairy Sci. 78 Suppl. 1 (1995) 145
    • (1995) J. Dairy Sci. , vol.78 , Issue.SUPPL. 1 , pp. 145
    • Esteves, C.L.1    Verissimo, P.C.2    Faro, C.J.3    Pires, E.V.4
  • 52
    • 0034763148 scopus 로고    scopus 로고
    • Mathematical modelling of the formation of rennet-induced gels by plant coagulants and chymosin
    • Esteves C.L.C., Lucey J.A., and Pires F.M.V. Mathematical modelling of the formation of rennet-induced gels by plant coagulants and chymosin. J. Dairy Res. 68 (2001) 499-510
    • (2001) J. Dairy Res. , vol.68 , pp. 499-510
    • Esteves, C.L.C.1    Lucey, J.A.2    Pires, F.M.V.3
  • 53
    • 0036098599 scopus 로고    scopus 로고
    • Rheological properties of milk gels made with coagulants of plant origin and chymosin
    • Esteves C.L.C., Lucey J.A., and Pires E.M.V. Rheological properties of milk gels made with coagulants of plant origin and chymosin. Int. Dairy J. 12 (2002) 427-434
    • (2002) Int. Dairy J. , vol.12 , pp. 427-434
    • Esteves, C.L.C.1    Lucey, J.A.2    Pires, E.M.V.3
  • 54
    • 0023735079 scopus 로고
    • Calcium-induced associations of the caseins - a thermodynamic linkage approach to precipitation and resolubilization
    • Farrell Jr. H.M., Kumosinski T.F., Pulaski P., and Thompson M.P. Calcium-induced associations of the caseins - a thermodynamic linkage approach to precipitation and resolubilization. Arch. Biochem. Biophys. 265 (1988) 146-158
    • (1988) Arch. Biochem. Biophys. , vol.265 , pp. 146-158
    • Farrell Jr., H.M.1    Kumosinski, T.F.2    Pulaski, P.3    Thompson, M.P.4
  • 55
    • 0035177887 scopus 로고    scopus 로고
    • Secondary structural studies of bovine caseins: temperature dependence of β-casein structure as analyzed by circular dichrosm and FTIR spectroscopy and correlation with micellization
    • Farrell Jr. H.M., Wickham E.D., Unruh J.J., Qi P.X., and Hoagland P.D. Secondary structural studies of bovine caseins: temperature dependence of β-casein structure as analyzed by circular dichrosm and FTIR spectroscopy and correlation with micellization. Food Hydrocolloids 15 (2001) 341-354
    • (2001) Food Hydrocolloids , vol.15 , pp. 341-354
    • Farrell Jr., H.M.1    Wickham, E.D.2    Unruh, J.J.3    Qi, P.X.4    Hoagland, P.D.5
  • 56
    • 0001103140 scopus 로고
    • On the enzymatic and coagulation stages of the renneting process
    • (London)
    • Foltmann B. On the enzymatic and coagulation stages of the renneting process. Proc. 15th Int. Dairy Congr. (London) (1959) 655-661
    • (1959) Proc. 15th Int. Dairy Congr. , pp. 655-661
    • Foltmann, B.1
  • 57
    • 0343883327 scopus 로고
    • The biochemistry of prorennin (prochymosin) and rennin (chymosin)
    • McKenzie H.A. (Ed), Academic Press, Cambridge
    • Foltmann B. The biochemistry of prorennin (prochymosin) and rennin (chymosin). In: McKenzie H.A. (Ed). Milk Proteins: Chemistry and Molecular Biology II (1971), Academic Press, Cambridge 217-254
    • (1971) Milk Proteins: Chemistry and Molecular Biology II , pp. 217-254
    • Foltmann, B.1
  • 58
    • 0006975896 scopus 로고
    • Ugeskrift Landmaend, 1870 Ser 3.9 341
    • Segeleke T., and Storch V. Ugeskrift Landmaend, 1870 Ser 3.9 341. Milchzeitung 3 (1874) 997
    • (1874) Milchzeitung , vol.3 , pp. 997
    • Segeleke, T.1    Storch, V.2
  • 59
    • 0026497631 scopus 로고
    • Chymosin: A short review on foetal and neonatal gastric proteases
    • Foltmann B. Chymosin: A short review on foetal and neonatal gastric proteases. Scand. J. Clin. Lab. Invest. 52 Suppl. 210 (1992) 65-79
    • (1992) Scand. J. Clin. Lab. Invest. , vol.52 , Issue.SUPPL. 210 , pp. 65-79
    • Foltmann, B.1
  • 60
    • 0002908192 scopus 로고    scopus 로고
    • Rennets: their role in milk coagulation and cheese ripening
    • Law B.A., and Davies F.L. (Eds), Blackie Academic and Professional, New York
    • Fox P.F., and McSweeney P.L.H. Rennets: their role in milk coagulation and cheese ripening. In: Law B.A., and Davies F.L. (Eds). Microbiology and Biochemistry of Cheese and Fermented Milk. 2nd edn (1997), Blackie Academic and Professional, New York 1-48
    • (1997) Microbiology and Biochemistry of Cheese and Fermented Milk. 2nd edn , pp. 1-48
    • Fox, P.F.1    McSweeney, P.L.H.2
  • 61
    • 0030894602 scopus 로고    scopus 로고
    • Combined effects of temperature and high-pressure treatments on physicochemical characteristics of skim milk
    • Gaucheron F., Famelart M.H., Mariette F., Raulot K., Michel F., and Le Graet Y. Combined effects of temperature and high-pressure treatments on physicochemical characteristics of skim milk. Food Chem. 59 (1997) 439-447
    • (1997) Food Chem. , vol.59 , pp. 439-447
    • Gaucheron, F.1    Famelart, M.H.2    Mariette, F.3    Raulot, K.4    Michel, F.5    Le Graet, Y.6
  • 62
    • 84974324303 scopus 로고
    • Density gradient electrophoresis of native and rennet-treated casein micelles
    • Green M.L., and Crutchfield G. Density gradient electrophoresis of native and rennet-treated casein micelles. J. Dairy Res. 38 (1971) 151-164
    • (1971) J. Dairy Res. , vol.38 , pp. 151-164
    • Green, M.L.1    Crutchfield, G.2
  • 63
    • 0000673110 scopus 로고
    • Secondary (nonenzymatic) phase of rennet coagulation and post-coagulation phenomenon
    • Fox P.F. (Ed), Chapman & Hall, London
    • Green M.L., and Grandison A.S. Secondary (nonenzymatic) phase of rennet coagulation and post-coagulation phenomenon. In: Fox P.F. (Ed). Cheese: Chemistry, Physics and Microbiology (1993), Chapman & Hall, London 101-140
    • (1993) Cheese: Chemistry, Physics and Microbiology , pp. 101-140
    • Green, M.L.1    Grandison, A.S.2
  • 64
    • 84971928492 scopus 로고
    • Intermicellar relationships in rennet-treated separated milk. II. Process of gel assembly
    • Green M.L., Hobbs D.G., Morant S.V., and Hill V.A. Intermicellar relationships in rennet-treated separated milk. II. Process of gel assembly. J. Dairy Res. 45 (1978) 413-422
    • (1978) J. Dairy Res. , vol.45 , pp. 413-422
    • Green, M.L.1    Hobbs, D.G.2    Morant, S.V.3    Hill, V.A.4
  • 65
    • 84974273885 scopus 로고
    • Cheddar cheesemaking with recombinant calf chymosin synthesised in Escherichia coli
    • Green M.L., Angal S., Lowe P.A., and Marston F.A.O. Cheddar cheesemaking with recombinant calf chymosin synthesised in Escherichia coli. J. Dairy Res. 52 (1985) 281-286
    • (1985) J. Dairy Res. , vol.52 , pp. 281-286
    • Green, M.L.1    Angal, S.2    Lowe, P.A.3    Marston, F.A.O.4
  • 67
    • 85032069834 scopus 로고
    • Rennet coagulation and coagulants used in cheese manufacture
    • Guinee T., and Wilkinson M. Rennet coagulation and coagulants used in cheese manufacture. J. Soc. Dairy Technol. 45 (1992) 94-104
    • (1992) J. Soc. Dairy Technol. , vol.45 , pp. 94-104
    • Guinee, T.1    Wilkinson, M.2
  • 68
    • 84972048023 scopus 로고
    • Observations on the primaryphase of milk coagulation by rennet under standardized conditions
    • Guthy K., and Novak G. Observations on the primaryphase of milk coagulation by rennet under standardized conditions. J. Dairy Res. 44 (1977) 363-366
    • (1977) J. Dairy Res. , vol.44 , pp. 363-366
    • Guthy, K.1    Novak, G.2
  • 69
    • 0009865639 scopus 로고
    • Chymogen, a chymosin rennet manufactured by fermentation of Aspergillus niger
    • International Dairy Federation, London
    • Harboe M.K. Chymogen, a chymosin rennet manufactured by fermentation of Aspergillus niger. Bulletin 269 (1992), International Dairy Federation, London 3-7
    • (1992) Bulletin , vol.269 , pp. 3-7
    • Harboe, M.K.1
  • 70
    • 0002874342 scopus 로고    scopus 로고
    • The production, action and application of rennet and coagulants
    • Law B.A. (Ed), Sheffield Academic Press, Brussels
    • Harboe M., and Budtz P. The production, action and application of rennet and coagulants. In: Law B.A. (Ed). Technology of Cheesemaking (1999), Sheffield Academic Press, Brussels 33-65
    • (1999) Technology of Cheesemaking , pp. 33-65
    • Harboe, M.1    Budtz, P.2
  • 71
    • 0000164409 scopus 로고
    • Application of reflection photometry to the measurement of milk coagulation
    • Hardy J., and Fanni J. Application of reflection photometry to the measurement of milk coagulation. J. Food Sci. 46 (1981) 1956-1957
    • (1981) J. Food Sci. , vol.46 , pp. 1956-1957
    • Hardy, J.1    Fanni, J.2
  • 72
    • 0010628911 scopus 로고
    • Use of recombinant chymosin in the manufacture of Cheddar and Colby cheese
    • Hicks C.L., O'Leary J., and Bucy J. Use of recombinant chymosin in the manufacture of Cheddar and Colby cheese. J. Dairy Sci. 71 (1988) 1127-1131
    • (1988) J. Dairy Sci. , vol.71 , pp. 1127-1131
    • Hicks, C.L.1    O'Leary, J.2    Bucy, J.3
  • 73
    • 0014430284 scopus 로고
    • The nature of the rennin sensitive bond in casein and its possible relation to sensitive bonds in other proteins
    • Hill R.D. The nature of the rennin sensitive bond in casein and its possible relation to sensitive bonds in other proteins. Biochem. Biophys. Res. Commun. 33 (1968) 659-663
    • (1968) Biochem. Biophys. Res. Commun. , vol.33 , pp. 659-663
    • Hill, R.D.1
  • 74
    • 0345396591 scopus 로고
    • Synthetic peptide and ester substrates for rennin
    • Hill R.D. Synthetic peptide and ester substrates for rennin. J. Dairy Res. 36 (1969) 409-415
    • (1969) J. Dairy Res. , vol.36 , pp. 409-415
    • Hill, R.D.1
  • 75
    • 0001744568 scopus 로고
    • The stability of casein micelles
    • Wolfram E. (Ed), Akademia Kiado, UK
    • Holt C. The stability of casein micelles. In: Wolfram E. (Ed). Proc. Int. Conf. Colloid Surface Science, Budapest Vol. 1 (1975), Akademia Kiado, UK 641-644
    • (1975) Proc. Int. Conf. Colloid Surface Science, Budapest , vol.1 , pp. 641-644
    • Holt, C.1
  • 76
    • 0001871181 scopus 로고    scopus 로고
    • The hairy casein micelle: evolution of the concept and its implications for dairy technology
    • Holt C., and Home D.S. The hairy casein micelle: evolution of the concept and its implications for dairy technology. Neth. Milk Dairy J. 50 (1996) 85-111
    • (1996) Neth. Milk Dairy J. , vol.50 , pp. 85-111
    • Holt, C.1    Home, D.S.2
  • 78
    • 0000360576 scopus 로고
    • Uber die labwirkung
    • Holter H. Uber die labwirkung. Biochem. Z. 255 (1932) 160-188
    • (1932) Biochem. Z. , vol.255 , pp. 160-188
    • Holter, H.1
  • 79
    • 84987367534 scopus 로고
    • Objective measurement of the process of curd formation during rennet treatment of milk by the hot wire method
    • Hori T. Objective measurement of the process of curd formation during rennet treatment of milk by the hot wire method. J. Food Sci. 50 (1985) 911-917
    • (1985) J. Food Sci. , vol.50 , pp. 911-917
    • Hori, T.1
  • 80
    • 0002997558 scopus 로고
    • Scaling behaviour of shear moduli during the formation of rennet milk gels
    • Dickinson E., and Lorient D. (Eds), Royal Society of Chemistry, Budapest
    • Home D.S. Scaling behaviour of shear moduli during the formation of rennet milk gels. In: Dickinson E., and Lorient D. (Eds). Food Macromolecules and Colloids (1995), Royal Society of Chemistry, Budapest 456-461
    • (1995) Food Macromolecules and Colloids , pp. 456-461
    • Home, D.S.1
  • 81
    • 0000842462 scopus 로고    scopus 로고
    • Aspects of scaling behaviour in the kinetics of particle gel formation
    • Home D.S. Aspects of scaling behaviour in the kinetics of particle gel formation. J. Chimie Phys. Phys.-chimie Biol. 93 (1996) 977-986
    • (1996) J. Chimie Phys. Phys.-chimie Biol. , vol.93 , pp. 977-986
    • Home, D.S.1
  • 82
    • 0032029213 scopus 로고    scopus 로고
    • Casein interactions: casting light on the black boxes, the structure in dairy products
    • Home D.S. Casein interactions: casting light on the black boxes, the structure in dairy products. Int. Dairy J. 8 (1998) 171-177
    • (1998) Int. Dairy J. , vol.8 , pp. 171-177
    • Home, D.S.1
  • 83
    • 0000868933 scopus 로고    scopus 로고
    • Factors influencing acid-induced gelation of skim milk
    • Dickinson E., and Miller R. (Eds), Royal Society of Chemistry, Cambridge
    • Home D.S. Factors influencing acid-induced gelation of skim milk. In: Dickinson E., and Miller R. (Eds). Food Colloids: Fundamentals of Formulation (2001), Royal Society of Chemistry, Cambridge 345-351
    • (2001) Food Colloids: Fundamentals of Formulation , pp. 345-351
    • Home, D.S.1
  • 84
    • 0036866003 scopus 로고    scopus 로고
    • Casein structure, self-assembly and gelation
    • Home D.S. Casein structure, self-assembly and gelation. Curr. Opin. Colloid. Inter J. Sci. 7 (2002) 456-461
    • (2002) Curr. Opin. Colloid. Inter J. Sci. , vol.7 , pp. 456-461
    • Home, D.S.1
  • 85
    • 0037433089 scopus 로고    scopus 로고
    • Casein micelles as hard spheres: limitations of the model in acidified gel formation
    • Home D.S. Casein micelles as hard spheres: limitations of the model in acidified gel formation. Colloids Surf. A: Physicochem. Eng. Aspects 213 (2003) 255-263
    • (2003) Colloids Surf. A: Physicochem. Eng. Aspects , vol.213 , pp. 255-263
    • Home, D.S.1
  • 86
    • 0001859507 scopus 로고
    • Direct observation of decrease in size of casein micelles during initial stages of renneting of skim milk
    • Home D.S., and Davidson C.M. Direct observation of decrease in size of casein micelles during initial stages of renneting of skim milk. Int. Dairy J. 3 (1993) 61-71
    • (1993) Int. Dairy J. , vol.3 , pp. 61-71
    • Home, D.S.1    Davidson, C.M.2
  • 88
    • 0036066607 scopus 로고    scopus 로고
    • Effects of high pressure on constituents and properties of milk
    • Huppertz T., Kelly A.L., and Fox P.F. Effects of high pressure on constituents and properties of milk. Int. Dairy J. 12 (2002) 561-572
    • (2002) Int. Dairy J. , vol.12 , pp. 561-572
    • Huppertz, T.1    Kelly, A.L.2    Fox, P.F.3
  • 89
    • 0002394361 scopus 로고
    • Enzymatically initiated coagulation of casein micelles: a kinetic model
    • Hyslop D.B. Enzymatically initiated coagulation of casein micelles: a kinetic model. Neth. Milk Dairy J. 43 (1989) 163-170
    • (1989) Neth. Milk Dairy J. , vol.43 , pp. 163-170
    • Hyslop, D.B.1
  • 90
    • 84976025775 scopus 로고
    • Enzyme-induced coagulation of casein micelles: a number of different kinetic models
    • Hyslop D.B. Enzyme-induced coagulation of casein micelles: a number of different kinetic models. J. Dairy Res. 60 (1993) 517-533
    • (1993) J. Dairy Res. , vol.60 , pp. 517-533
    • Hyslop, D.B.1
  • 91
    • 4043148450 scopus 로고    scopus 로고
    • Enzymatic coagulation of milk
    • Fox P.F., and McSweeney P.L.H. (Eds), Kluwer, Cambridge
    • Hyslop D.B. Enzymatic coagulation of milk. In: Fox P.F., and McSweeney P.L.H. (Eds). Advanced Dairy Chemistry I. Proteins. 3rd edn (2003), Kluwer, Cambridge 835-874
    • (2003) Advanced Dairy Chemistry I. Proteins. 3rd edn , pp. 835-874
    • Hyslop, D.B.1
  • 92
    • 0000481111 scopus 로고    scopus 로고
    • Application of numerical analysis to a number of models for chymosininduced coagulation of casein micelles
    • Hyslop D.B., and Qvist K.B. Application of numerical analysis to a number of models for chymosininduced coagulation of casein micelles. J. Dairy Res. 63 (1996) 223-232
    • (1996) J. Dairy Res. , vol.63 , pp. 223-232
    • Hyslop, D.B.1    Qvist, K.B.2
  • 94
    • 33748892757 scopus 로고
    • Scaling of kinetically growing clusters
    • Kolb M., Botet R., and Jullien R. Scaling of kinetically growing clusters. Phys. Rev. Lett. 51 (1983) 1123-1126
    • (1983) Phys. Rev. Lett. , vol.51 , pp. 1123-1126
    • Kolb, M.1    Botet, R.2    Jullien, R.3
  • 95
    • 0000028392 scopus 로고    scopus 로고
    • Comparisons of the effects of high pressure and thermal treatments on the casein micelles in goats milk
    • Law A.J.R., Leaver J., Felipe X., Ferragut V., Pla R., and Guamis B. Comparisons of the effects of high pressure and thermal treatments on the casein micelles in goats milk. J. Agric. Food Chem. 46 (1998) 2523-2530
    • (1998) J. Agric. Food Chem. , vol.46 , pp. 2523-2530
    • Law, A.J.R.1    Leaver, J.2    Felipe, X.3    Ferragut, V.4    Pla, R.5    Guamis, B.6
  • 96
    • 0001071614 scopus 로고
    • Influence of heating regime and pH on the primary phase of renneting of whole milk
    • Leaver J., Law A.J.R., Home D.S., and Banks J.M. Influence of heating regime and pH on the primary phase of renneting of whole milk. Int. Dairy J. 5 (1995) 129-140
    • (1995) Int. Dairy J. , vol.5 , pp. 129-140
    • Leaver, J.1    Law, A.J.R.2    Home, D.S.3    Banks, J.M.4
  • 98
    • 0030687564 scopus 로고    scopus 로고
    • Relationship between rheological properties and degree of κ-casein proteolysis during renneting of milk
    • Lomholt S.B., and Qvist K.B. Relationship between rheological properties and degree of κ-casein proteolysis during renneting of milk. J. Dairy Res. 64 (1997) 541-549
    • (1997) J. Dairy Res. , vol.64 , pp. 541-549
    • Lomholt, S.B.1    Qvist, K.B.2
  • 99
    • 0002511635 scopus 로고    scopus 로고
    • The formation of cheese curd
    • Law B.A. (Ed), Sheffield Academic Press, Brussels
    • Lomholt S.B., and Qvist K.B. The formation of cheese curd. In: Law B.A. (Ed). The Technology of Cheesemaking (1999), Sheffield Academic Press, Brussels 66-98
    • (1999) The Technology of Cheesemaking , pp. 66-98
    • Lomholt, S.B.1    Qvist, K.B.2
  • 100
    • 0031725770 scopus 로고    scopus 로고
    • Kinetics of renneting reaction followed by measurement of turbidity as a function of wavelength
    • Lomholt S.B., Worning P., Øgendal L., Qvist K.B., Hyslop D.B., and Bauer R. Kinetics of renneting reaction followed by measurement of turbidity as a function of wavelength. J. Dairy Res. 65 (1998) 545-554
    • (1998) J. Dairy Res. , vol.65 , pp. 545-554
    • Lomholt, S.B.1    Worning, P.2    Øgendal, L.3    Qvist, K.B.4    Hyslop, D.B.5    Bauer, R.6
  • 101
    • 0032049514 scopus 로고    scopus 로고
    • Rheological properties and cutting time of rennet gels: effect ofpH and enzyme concentration
    • Lopez M.B., Lomholt S.B., and Qvist K.B. Rheological properties and cutting time of rennet gels: effect ofpH and enzyme concentration. Int. Dairy J. 8 (1998) 289-293
    • (1998) Int. Dairy J. , vol.8 , pp. 289-293
    • Lopez, M.B.1    Lomholt, S.B.2    Qvist, K.B.3
  • 102
    • 0032125334 scopus 로고    scopus 로고
    • Effects of high pressures combined with moderate temperatures on the rennet coagulation properties of milk
    • Lopez-Fandino R., and Olano A. Effects of high pressures combined with moderate temperatures on the rennet coagulation properties of milk. Int. Dairy J. 8 (1998) 623-627
    • (1998) Int. Dairy J. , vol.8 , pp. 623-627
    • Lopez-Fandino, R.1    Olano, A.2
  • 103
    • 0038987330 scopus 로고    scopus 로고
    • The effects of high pressure on whey protein denaturationand cheesemaking properties of raw milk
    • Lopez-Fandino R., Carracosa A.V., and Olano A. The effects of high pressure on whey protein denaturationand cheesemaking properties of raw milk. J. Dairy Sci. 79 (1996) 929-936
    • (1996) J. Dairy Sci. , vol.79 , pp. 929-936
    • Lopez-Fandino, R.1    Carracosa, A.V.2    Olano, A.3
  • 104
    • 0642315405 scopus 로고    scopus 로고
    • Rennet coagulation of milk subjected to high pressures
    • Lopez-Fandino R., Ramos M., and Olano A. Rennet coagulation of milk subjected to high pressures. J. Agric. Food Chem. 45 (1997) 3233-3237
    • (1997) J. Agric. Food Chem. , vol.45 , pp. 3233-3237
    • Lopez-Fandino, R.1    Ramos, M.2    Olano, A.3
  • 105
    • 0040497022 scopus 로고    scopus 로고
    • Distribution of minerals and proteins between the soluble and colloidal phases of pressurised milks from different species
    • Lopez-Fandino R., de la Fuente M.A., Ramos M., and Olano A. Distribution of minerals and proteins between the soluble and colloidal phases of pressurised milks from different species. J. Dairy Res. 65 (1998) 69-78
    • (1998) J. Dairy Res. , vol.65 , pp. 69-78
    • Lopez-Fandino, R.1    de la Fuente, M.A.2    Ramos, M.3    Olano, A.4
  • 106
    • 1642601815 scopus 로고    scopus 로고
    • Formation and physical properties of milk protein gels
    • Lucey J.A. Formation and physical properties of milk protein gels. J. Dairy Sci. 85 (2002) 281-294
    • (2002) J. Dairy Sci. , vol.85 , pp. 281-294
    • Lucey, J.A.1
  • 108
    • 0002799525 scopus 로고
    • Physico-chemical properties of casein micelles reformed from urea-treated milk
    • McGann T.C.A., and Fox P.F. Physico-chemical properties of casein micelles reformed from urea-treated milk. J. Dairy Res. 41 (1974) 45-53
    • (1974) J. Dairy Res. , vol.41 , pp. 45-53
    • McGann, T.C.A.1    Fox, P.F.2
  • 109
    • 0000350748 scopus 로고
    • Formation of fractal clusters and networks by irreversible diffusion-limited aggregation
    • Meakin P. Formation of fractal clusters and networks by irreversible diffusion-limited aggregation. Phys. Rev. Lett. 51 (1983) 1119-1122
    • (1983) Phys. Rev. Lett. , vol.51 , pp. 1119-1122
    • Meakin, P.1
  • 110
    • 0003794960 scopus 로고    scopus 로고
    • Scaling Relations between Structure and Rheology of Ageing Casein Particle Gels
    • Wageningen, The Netherlands.
    • Wageningen, The Netherlands. Mellema M. Scaling Relations between Structure and Rheology of Ageing Casein Particle Gels. PhD Thesis, Wageningen University (2000)
    • (2000) PhD Thesis, Wageningen University
    • Mellema, M.1
  • 111
    • 0034247906 scopus 로고    scopus 로고
    • Structure and scaling behaviour of aging rennet-induced casein gels examined by confocal microscopy and permeametry
    • Mellema M., Heesakkers J.W.M., Van Opheusden J.H.J., and Van Vliet T. Structure and scaling behaviour of aging rennet-induced casein gels examined by confocal microscopy and permeametry. Langmuir 16 (2000) 6847-6854
    • (2000) Langmuir , vol.16 , pp. 6847-6854
    • Mellema, M.1    Heesakkers, J.W.M.2    Van Opheusden, J.H.J.3    Van Vliet, T.4
  • 112
    • 0037177375 scopus 로고    scopus 로고
    • Effects of structural rearrangements on the rheology of rennet-induced casein particle gels
    • Mellema M., Walstra P., Van Opheusden J.H.J., and Van Vliet T. Effects of structural rearrangements on the rheology of rennet-induced casein particle gels. Adv. Colloid Interf. Sci. 98 (2002) 25-50
    • (2002) Adv. Colloid Interf. Sci. , vol.98 , pp. 25-50
    • Mellema, M.1    Walstra, P.2    Van Opheusden, J.H.J.3    Van Vliet, T.4
  • 113
    • 0019400281 scopus 로고
    • Phosphorylation of caseins: present evidence for an amino acid triplet code posttranslationally recognized by specific kinases
    • Mercier J.C. Phosphorylation of caseins: present evidence for an amino acid triplet code posttranslationally recognized by specific kinases. Biochimie 63 (1981) 1-17
    • (1981) Biochimie , vol.63 , pp. 1-17
    • Mercier, J.C.1
  • 114
    • 0001509510 scopus 로고
    • The rennet hysteresis of heated milk
    • Morrissey P.A. The rennet hysteresis of heated milk. J. Dairy Res. 36 (1969) 333-341
    • (1969) J. Dairy Res. , vol.36 , pp. 333-341
    • Morrissey, P.A.1
  • 115
    • 0034141225 scopus 로고    scopus 로고
    • High pressure treatment of milk: effects on casein micelle structure and on enzymic coagulation
    • Needs E.C., Stenning R.A., Gill A.L., Ferragut V., and Rich G.T. High pressure treatment of milk: effects on casein micelle structure and on enzymic coagulation. J. Dairy Res. 67 (2000) 31-42
    • (2000) J. Dairy Res. , vol.67 , pp. 31-42
    • Needs, E.C.1    Stenning, R.A.2    Gill, A.L.3    Ferragut, V.4    Rich, G.T.5
  • 116
    • 0642328156 scopus 로고
    • Physical properties of gels and microstructure of rennet gels from casein micelles of different sizes
    • Niki R., Kim G.Y., Kimura T., Takahashi K., Kohyama K., and Nishinari K. Physical properties of gels and microstructure of rennet gels from casein micelles of different sizes. Milchwissenschaft 49 (1994) 325-329
    • (1994) Milchwissenschaft , vol.49 , pp. 325-329
    • Niki, R.1    Kim, G.Y.2    Kimura, T.3    Takahashi, K.4    Kohyama, K.5    Nishinari, K.6
  • 117
  • 118
    • 33751406321 scopus 로고
    • Factors affecting cheese yields
    • 19.
    • 19. Olson N.F. Factors affecting cheese yields. Dairy Ind. Int. 42 (1977) 14-15
    • (1977) Dairy Ind. Int. , vol.42 , pp. 14-15
    • Olson, N.F.1
  • 120
    • 0019525601 scopus 로고
    • Binding of calcium ions to bovine β-casein
    • Parker T.G., and Dalgleish D.G. Binding of calcium ions to bovine β-casein. J. Dairy Res. 48 (1981) 71-76
    • (1981) J. Dairy Res. , vol.48 , pp. 71-76
    • Parker, T.G.1    Dalgleish, D.G.2
  • 121
    • 0012210909 scopus 로고
    • On the enzyme-triggered clotting of casein: a preliminary account
    • Payens T.A.J. On the enzyme-triggered clotting of casein: a preliminary account. Neth. Milk Dairy J. 30 (1976) 55-59
    • (1976) Neth. Milk Dairy J. , vol.30 , pp. 55-59
    • Payens, T.A.J.1
  • 122
    • 0017386849 scopus 로고
    • On enzymatic clotting processes. II. The colloidal instability of chymosin-treated casein micelles
    • Payens T.A.J. On enzymatic clotting processes. II. The colloidal instability of chymosin-treated casein micelles. Biophys. Chem. 6 (1977) 263-270
    • (1977) Biophys. Chem. , vol.6 , pp. 263-270
    • Payens, T.A.J.1
  • 123
    • 0018461686 scopus 로고
    • Casein micelles: the colloid-chemical approach
    • Payens T.A.J. Casein micelles: the colloid-chemical approach. J. Dairy Res. 46 (1979) 291-306
    • (1979) J. Dairy Res. , vol.46 , pp. 291-306
    • Payens, T.A.J.1
  • 124
    • 0001865626 scopus 로고
    • The enzyme-triggered coagulation of casein micelles
    • Payens T.A.J. The enzyme-triggered coagulation of casein micelles. Adv. Colloid Interf. Sci. 30 (1989) 31-69
    • (1989) Adv. Colloid Interf. Sci. , vol.30 , pp. 31-69
    • Payens, T.A.J.1
  • 125
    • 0022779909 scopus 로고
    • Mean-field kinetics of the enzyme-triggered gelation of casein micelles
    • Payens T.A.J., and Brinkhuis J. Mean-field kinetics of the enzyme-triggered gelation of casein micelles. Colloids Surf. 20 (1986) 31-69
    • (1986) Colloids Surf. , vol.20 , pp. 31-69
    • Payens, T.A.J.1    Brinkhuis, J.2
  • 126
    • 0014484073 scopus 로고
    • Self-association in non-ideal systems. Combined light-scattering and sedimentation measurements in β-casein solutions
    • Payens T.A.J., Brinkhuis J.A., and Van Markwijk B.W. Self-association in non-ideal systems. Combined light-scattering and sedimentation measurements in β-casein solutions. Biochim. Biophys. Acta 175 (1969) 434-437
    • (1969) Biochim. Biophys. Acta , vol.175 , pp. 434-437
    • Payens, T.A.J.1    Brinkhuis, J.A.2    Van Markwijk, B.W.3
  • 127
    • 0017377897 scopus 로고
    • On enzymatic clotting processes. 1. Kinetics of enzymetriggered coagulation reactions
    • Payens T.A.J., Wiersma A.K., and Brinkhuis J. On enzymatic clotting processes. 1. Kinetics of enzymetriggered coagulation reactions. Biophys. Chem. 6 (1977) 253-261
    • (1977) Biophys. Chem. , vol.6 , pp. 253-261
    • Payens, T.A.J.1    Wiersma, A.K.2    Brinkhuis, J.3
  • 128
    • 84974410190 scopus 로고
    • Moving boundary electrophoresis of native and rennet-treated casein micelles
    • Pearse K.N. Moving boundary electrophoresis of native and rennet-treated casein micelles. J. Dairy Res. 43 (1976) 27-36
    • (1976) J. Dairy Res. , vol.43 , pp. 27-36
    • Pearse, K.N.1
  • 129
    • 0015443890 scopus 로고
    • Studies on the specificity of chymosin (rennin). I. Kinetic parameters of the hydrolysis of synthetic oligopeptide substrates
    • Raymond M.N., Gamier J., Bricas E., Cilianu S., Blasnic M., Chain A., and Lefrancier P. Studies on the specificity of chymosin (rennin). I. Kinetic parameters of the hydrolysis of synthetic oligopeptide substrates. Biochimie 54 (1972) 145-154
    • (1972) Biochimie , vol.54 , pp. 145-154
    • Raymond, M.N.1    Gamier, J.2    Bricas, E.3    Cilianu, S.4    Blasnic, M.5    Chain, A.6    Lefrancier, P.7
  • 131
    • 84986736567 scopus 로고
    • Rheological characterization of gels
    • Ross Murphy S.B. Rheological characterization of gels. J. Texture Studies 26 (1995) 391-400
    • (1995) J. Texture Studies , vol.26 , pp. 391-400
    • Ross Murphy, S.B.1
  • 133
    • 79551584433 scopus 로고
    • Physical changes in milk caused by the action of rennet
    • Scott Blair G.W., and Burnett J. Physical changes in milk caused by the action of rennet. J. Dairy Res. 25 (1958) 297-303
    • (1958) J. Dairy Res. , vol.25 , pp. 297-303
    • Scott Blair, G.W.1    Burnett, J.2
  • 134
    • 84971961725 scopus 로고
    • A viscometric study of the breakdown of casein in milk by rennin and rennet
    • Scott Blair G.W., and Oosthuizen J.C. A viscometric study of the breakdown of casein in milk by rennin and rennet. J. Dairy Res. 28 (1961) 165-173
    • (1961) J. Dairy Res. , vol.28 , pp. 165-173
    • Scott Blair, G.W.1    Oosthuizen, J.C.2
  • 135
    • 0000153940 scopus 로고
    • Proteolytic activity of some milk-clotting enzymes on κ-casein
    • Shammet K.M., Brown R.J., and McMahon D.J. Proteolytic activity of some milk-clotting enzymes on κ-casein. J. Dairy Sci. 75 (1992) 1373-1379
    • (1992) J. Dairy Sci. , vol.75 , pp. 1373-1379
    • Shammet, K.M.1    Brown, R.J.2    McMahon, D.J.3
  • 136
    • 0001024684 scopus 로고
    • Scaling behaviour of the elastic properties of colloidal gels
    • Shih W.H., Shih W.Y., Kim S.I., Liu J., and Aksay I.A. Scaling behaviour of the elastic properties of colloidal gels. Phys. Rev. A 42 (1990) 4772-4779
    • (1990) Phys. Rev. A , vol.42 , pp. 4772-4779
    • Shih, W.H.1    Shih, W.Y.2    Kim, S.I.3    Liu, J.4    Aksay, I.A.5
  • 137
    • 0034864555 scopus 로고    scopus 로고
    • Influence of heat treatment of milk on cheesemaking properties
    • Singh H., and Waungana A. Influence of heat treatment of milk on cheesemaking properties. Int. Dairy J. 11 (2001) 543-551
    • (2001) Int. Dairy J. , vol.11 , pp. 543-551
    • Singh, H.1    Waungana, A.2
  • 138
    • 0034870511 scopus 로고    scopus 로고
    • Advances in the study of proteolysis during cheese ripening
    • Sousa M.J., Ardo Y., and McSweeney P.L.H. Advances in the study of proteolysis during cheese ripening. Int. Dairy J. 11 (2001) 327-343
    • (2001) Int. Dairy J. , vol.11 , pp. 327-343
    • Sousa, M.J.1    Ardo, Y.2    McSweeney, P.L.H.3
  • 139
    • 0344888259 scopus 로고
    • Gelation in concentrated critically branched polymer solutions. Percolation theory of intramolecular bond cycles
    • Stauffer D. Gelation in concentrated critically branched polymer solutions. Percolation theory of intramolecular bond cycles. J. Chem. Soc. Faraday Trans. II 72 (1976) 1354-1364
    • (1976) J. Chem. Soc. Faraday Trans. II , vol.72 , pp. 1354-1364
    • Stauffer, D.1
  • 140
    • 2442700864 scopus 로고
    • Theory of molecular size distribution and gel formation in branched chain polymers
    • Stockmayer W.H. Theory of molecular size distribution and gel formation in branched chain polymers. J. Chem. Phys. 11 (1943) 45-55
    • (1943) J. Chem. Phys. , vol.11 , pp. 45-55
    • Stockmayer, W.H.1
  • 141
    • 0002772383 scopus 로고
    • Chemistry of the caseins
    • Fox P.F. (Ed), London, Elsevier Applied Science
    • Swaisgood H.E. Chemistry of the caseins. In: Fox P.F. (Ed). Advanced Dairy Chemistry. 1. Proteins (1992), London, Elsevier Applied Science 63-110
    • (1992) Advanced Dairy Chemistry. 1. Proteins , pp. 63-110
    • Swaisgood, H.E.1
  • 142
    • 0036157963 scopus 로고    scopus 로고
    • A Raman optical activity study of rheomorphism in caseins, synucleins and tau: new insight into the structure and behaviour of natively unfolded proteins
    • Syme C.D., Blanch E.W., Holt C., Jakes R., Goedert M., Hecht L., and Barron L.D. A Raman optical activity study of rheomorphism in caseins, synucleins and tau: new insight into the structure and behaviour of natively unfolded proteins. Fur. J. Biochem. 269 (2002) 148-156
    • (2002) Fur. J. Biochem. , vol.269 , pp. 148-156
    • Syme, C.D.1    Blanch, E.W.2    Holt, C.3    Jakes, R.4    Goedert, M.5    Hecht, L.6    Barron, L.D.7
  • 143
    • 0040196421 scopus 로고
    • Production of chymosin (E.C.3.4.23.4) by microorganisms and its use for cheesemaking
    • International Dairy Federation
    • Teuber M. Production of chymosin (E.C.3.4.23.4) by microorganisms and its use for cheesemaking. Bulletin 251 (1990), International Dairy Federation 3-15
    • (1990) Bulletin , vol.251 , pp. 3-15
    • Teuber, M.1
  • 144
    • 85025556211 scopus 로고
    • Gelation mechanism and percolation
    • Tokita M. Gelation mechanism and percolation. Food Hydrocolloids 3 (1989) 263-274
    • (1989) Food Hydrocolloids , vol.3 , pp. 263-274
    • Tokita, M.1
  • 145
    • 0019972708 scopus 로고
    • Dynamic viscoelastic studies on the mechanism of milk clotting process
    • Tokita M.K., Kikichi R., Niki R., and Arima S. Dynamic viscoelastic studies on the mechanism of milk clotting process. Biorheology 19 (1982) 209-219
    • (1982) Biorheology , vol.19 , pp. 209-219
    • Tokita, M.K.1    Kikichi, R.2    Niki, R.3    Arima, S.4
  • 147
    • 0036890035 scopus 로고    scopus 로고
    • Applications of high-hydrostatic pressure on milk and dairy products - a review. Innov
    • Trujillo A.J., Capellas M., Saldo J., Gervilla R., and Guamis B. Applications of high-hydrostatic pressure on milk and dairy products - a review. Innov. Food Sci. Fmerg Technol. 3 (2002) 295-307
    • (2002) Food Sci. Fmerg Technol. , vol.3 , pp. 295-307
    • Trujillo, A.J.1    Capellas, M.2    Saldo, J.3    Gervilla, R.4    Guamis, B.5
  • 148
    • 84974274823 scopus 로고
    • A kinetic model of the clotting of casein by rennet
    • Tuszynski W.B. A kinetic model of the clotting of casein by rennet. J. Dairy Res. 38 (1971) 113-125
    • (1971) J. Dairy Res. , vol.38 , pp. 113-125
    • Tuszynski, W.B.1
  • 149
    • 0346744134 scopus 로고
    • Effect of milk clotting enzymes on cheese yield
    • Ustinol Z., and Hicks C.L. Effect of milk clotting enzymes on cheese yield. J. Dairy Sci. 73 (1990) 8-19
    • (1990) J. Dairy Sci. , vol.73 , pp. 8-19
    • Ustinol, Z.1    Hicks, C.L.2
  • 150
    • 84985209689 scopus 로고
    • Diffuse reflectance profiles of eight milk clotting enzyme preparations
    • Ustinol Z., Hicks C.L., and Payne F.A. Diffuse reflectance profiles of eight milk clotting enzyme preparations. J. Food Sci. 56 (1991) 411-415
    • (1991) J. Food Sci. , vol.56 , pp. 411-415
    • Ustinol, Z.1    Hicks, C.L.2    Payne, F.A.3
  • 151
    • 0002779639 scopus 로고
    • Fermentation produced chymosin: technological aspects of its use for cheesemaking
    • International Dairy Federation, Brussels
    • Van den Berg G. Fermentation produced chymosin: technological aspects of its use for cheesemaking. Bulletin 269 (1992), International Dairy Federation, Brussels 13-17
    • (1992) Bulletin , vol.269 , pp. 13-17
    • Van den Berg, G.1
  • 152
    • 0001788441 scopus 로고
    • Interpretation of the kinetics of the renneting reaction in milk
    • Van Hooydonk A.C.M., and Walstra P. Interpretation of the kinetics of the renneting reaction in milk. Neth. Milk Dairy J. 41 (1987) 19-47
    • (1987) Neth. Milk Dairy J. , vol.41 , pp. 19-47
    • Van Hooydonk, A.C.M.1    Walstra, P.2
  • 153
    • 0000613966 scopus 로고
    • pH-induced physico-chemical changes of casein micelles in milk and their effect on renneting. 1. Effect of pH on renneting of milk
    • Van Hooydonk A.C.M., Boerrigter I.J., and Hagedoorn H.G. pH-induced physico-chemical changes of casein micelles in milk and their effect on renneting. 1. Effect of pH on renneting of milk. Neth. Milk Dairy J. 40 (1986) 297-313
    • (1986) Neth. Milk Dairy J. , vol.40 , pp. 297-313
    • Van Hooydonk, A.C.M.1    Boerrigter, I.J.2    Hagedoorn, H.G.3
  • 155
    • 0009018212 scopus 로고
    • Note on the shear modulus of rennet-induced milk gels
    • Van Vliet T., and WalstraT P. Note on the shear modulus of rennet-induced milk gels. Neth. Milk Dairy J. 39 (1985) 115-118
    • (1985) Neth. Milk Dairy J. , vol.39 , pp. 115-118
    • Van Vliet, T.1    WalstraT, P.2
  • 156
    • 0026169038 scopus 로고
    • Relation between syneresis and rheological properties of particle gels
    • Van Vliet T., Van Dijk H.J.M., Zoon P., and Walstra P. Relation between syneresis and rheological properties of particle gels. Colloid Polym. Sci. 269 (1991) 620-627
    • (1991) Colloid Polym. Sci. , vol.269 , pp. 620-627
    • Van Vliet, T.1    Van Dijk, H.J.M.2    Zoon, P.3    Walstra, P.4
  • 157
    • 0029018457 scopus 로고
    • The vegetable rennet of Cyanara cardunculus L. contains two proteinases with chymosin and pepsin-like specificities
    • Verissimo P.C., Esteves C.L.C., Faro C.J.F., and Pires E.M.V. The vegetable rennet of Cyanara cardunculus L. contains two proteinases with chymosin and pepsin-like specificities. Biotechnol. Lett. 17 (1995) 621-626
    • (1995) Biotechnol. Lett. , vol.17 , pp. 621-626
    • Verissimo, P.C.1    Esteves, C.L.C.2    Faro, C.J.F.3    Pires, E.M.V.4
  • 159
    • 0019125977 scopus 로고
    • Peptide substrates for chymosin (rennin). Isolation and substrate behaviour of two tryptic fragments of bovine κ-casein
    • Visser S., Van Roijen P.J., and Slangen C.J. Peptide substrates for chymosin (rennin). Isolation and substrate behaviour of two tryptic fragments of bovine κ-casein. Eur. J. Biochem. 108 (1980) 415-421
    • (1980) Eur. J. Biochem. , vol.108 , pp. 415-421
    • Visser, S.1    Van Roijen, P.J.2    Slangen, C.J.3
  • 160
    • 0018462333 scopus 로고
    • The association of bovine SH-κ-casein at pH 7.0
    • Vreeman H.J. The association of bovine SH-κ-casein at pH 7.0. J. Dairy Res. 46 (1979) 271-276
    • (1979) J. Dairy Res. , vol.46 , pp. 271-276
    • Vreeman, H.J.1
  • 162
    • 0023050655 scopus 로고
    • Characterization of bovine κ-casein fractions and the kinetics of chymosin-induced macropeptide release from carbohydrate-free and carbohydrate-containing fractions determined by high performance gel permeation chromatography
    • Vreeman H.J., Visser S., Slangen C.J., and Van Riel J.A.M. Characterization of bovine κ-casein fractions and the kinetics of chymosin-induced macropeptide release from carbohydrate-free and carbohydrate-containing fractions determined by high performance gel permeation chromatography. Biochem. J. 240 (1986) 87-97
    • (1986) Biochem. J. , vol.240 , pp. 87-97
    • Vreeman, H.J.1    Visser, S.2    Slangen, C.J.3    Van Riel, J.A.M.4
  • 163
    • 0018463574 scopus 로고
    • The voluminosity of casein micelles and some of its implication
    • Walstra P. The voluminosity of casein micelles and some of its implication. J. Dairy Res. 46 (1979) 317-323
    • (1979) J. Dairy Res. , vol.46 , pp. 317-323
    • Walstra, P.1
  • 164
    • 0000569617 scopus 로고
    • The physical chemistry of curd making
    • Walstra P., and Van Vliet T. The physical chemistry of curd making. Neth. Milk Dairy J. 40 (1986) 241-259
    • (1986) Neth. Milk Dairy J. , vol.40 , pp. 241-259
    • Walstra, P.1    Van Vliet, T.2
  • 165
    • 0019890187 scopus 로고
    • Effect of chymosin action on the hydrodynamic diameter of casein micelles
    • Walstra P., Bloomfield V.A., Wei G.J., and Jenness R. Effect of chymosin action on the hydrodynamic diameter of casein micelles. Biochim. Biophys. Acta 669 (1981) 258-259
    • (1981) Biochim. Biophys. Acta , vol.669 , pp. 258-259
    • Walstra, P.1    Bloomfield, V.A.2    Wei, G.J.3    Jenness, R.4
  • 166
    • 0030437488 scopus 로고    scopus 로고
    • Influence of denaturation and aggregation of beta-lactoglobulin on rennet coagulation properties of skim milk and ultrafiltered milk
    • Waungana A., Singh H., and Bennett R.J. Influence of denaturation and aggregation of beta-lactoglobulin on rennet coagulation properties of skim milk and ultrafiltered milk. Food Res. Int. 29 (1996) 715-721
    • (1996) Food Res. Int. , vol.29 , pp. 715-721
    • Waungana, A.1    Singh, H.2    Bennett, R.J.3
  • 167
    • 0006263578 scopus 로고
    • Proteins of milk
    • Wong N.P. (Ed), Avi Books, Van Norstrand Reinhold, Amsterdam
    • Whitney R.McL. Proteins of milk. In: Wong N.P. (Ed). Fundamentals of Dairy Chemistry. 3rd edn (1988), Avi Books, Van Norstrand Reinhold, Amsterdam 81-169
    • (1988) Fundamentals of Dairy Chemistry. 3rd edn , pp. 81-169
    • Whitney, R.McL.1
  • 168
    • 0000441076 scopus 로고    scopus 로고
    • Cheese and whey
    • Godfrey T., and West S. (Eds), MacMillan Press, New York
    • Wigley R.C. Cheese and whey. In: Godfrey T., and West S. (Eds). Industrial Enzymology. 2nd edn (1996), MacMillan Press, New York 133-154
    • (1996) Industrial Enzymology. 2nd edn , pp. 133-154
    • Wigley, R.C.1
  • 169
    • 0022694827 scopus 로고
    • Analysis of cross-linked polymer at the gel-point
    • Winter H.H., and Chambon F. Analysis of cross-linked polymer at the gel-point. J. Rheology 30 (1986) 367-382
    • (1986) J. Rheology , vol.30 , pp. 367-382
    • Winter, H.H.1    Chambon, F.2
  • 170
    • 0032527383 scopus 로고    scopus 로고
    • A novel approach to turbidimetry of dense systems. An investigation of the enzymatic gelation of casein micelles
    • Worning P., Bauer R., Øgendal L., and Lomholt S. A novel approach to turbidimetry of dense systems. An investigation of the enzymatic gelation of casein micelles. J. Colloid Interf. Sci. 203 (1998) 265-277
    • (1998) J. Colloid Interf. Sci. , vol.203 , pp. 265-277
    • Worning, P.1    Bauer, R.2    Øgendal, L.3    Lomholt, S.4
  • 171
    • 0002524551 scopus 로고
    • A study of the carbohydrate binding sites of bovine κ-casein using high performance liquid chromatography
    • Zevaco C., and Ribadeau-Dumas B. A study of the carbohydrate binding sites of bovine κ-casein using high performance liquid chromatography. Milchwissenschaft 39 (1984) 206-210
    • (1984) Milchwissenschaft , vol.39 , pp. 206-210
    • Zevaco, C.1    Ribadeau-Dumas, B.2
  • 172
    • 0000468574 scopus 로고
    • Kinetics of polymerization
    • Ziff R.M. Kinetics of polymerization. J. Stat. Phys. 23 (1980) 241-263
    • (1980) J. Stat. Phys. , vol.23 , pp. 241-263
    • Ziff, R.M.1
  • 173
    • 36749105754 scopus 로고
    • Kinetics of polymer gelation
    • Ziff R.M., and Stell G. Kinetics of polymer gelation. J. Chem. Phys. 73 (1982) 3492-3499
    • (1982) J. Chem. Phys. , vol.73 , pp. 3492-3499
    • Ziff, R.M.1    Stell, G.2
  • 174
    • 0000563721 scopus 로고
    • Rheological properties of rennet-induced skim milk gels. 1. Introduction
    • Zoon P., Van Vliet T., and Walstra P. Rheological properties of rennet-induced skim milk gels. 1. Introduction. Neth. Milk Dairy J. 42 (1988) 249-269
    • (1988) Neth. Milk Dairy J. , vol.42 , pp. 249-269
    • Zoon, P.1    Van Vliet, T.2    Walstra, P.3
  • 175
    • 0000505358 scopus 로고
    • Rheological properties of rennet-induced skim milk gels. 2. Effect of temperature
    • Zoon P., Van Vliet T., and Walstra P. Rheological properties of rennet-induced skim milk gels. 2. Effect of temperature. Neth. Milk Dairy J. 42 (1988) 271-294
    • (1988) Neth. Milk Dairy J. , vol.42 , pp. 271-294
    • Zoon, P.1    Van Vliet, T.2    Walstra, P.3
  • 176
    • 0003309463 scopus 로고
    • Rheological properties of rennet-induced skim milk gels. 3. Effect of calcium and phosphate
    • Zoon P., Van Vliet T., and Walstra P. Rheological properties of rennet-induced skim milk gels. 3. Effect of calcium and phosphate. Neth. Milk Dairy J. 42 (1988) 295-312
    • (1988) Neth. Milk Dairy J. , vol.42 , pp. 295-312
    • Zoon, P.1    Van Vliet, T.2    Walstra, P.3
  • 177
    • 0002350215 scopus 로고
    • Rheological properties of rennet-induced skim milk gels. 4. The effect of pH and NaCl
    • Zoon P., Van Vliet T., and Walstra P. Rheological properties of rennet-induced skim milk gels. 4. The effect of pH and NaCl. Neth. Milk Dairy J. 43 (1989) 17-34
    • (1989) Neth. Milk Dairy J. , vol.43 , pp. 17-34
    • Zoon, P.1    Van Vliet, T.2    Walstra, P.3
  • 178
    • 1542554993 scopus 로고
    • Rheological properties of rennet-induced skim milk gels. 5. Behaviour at large deformation
    • Zoon P., Van Vliet T., and Walstra P. Rheological properties of rennet-induced skim milk gels. 5. Behaviour at large deformation. Neth. Milk Dairy J. 43 (1989) 35-42
    • (1989) Neth. Milk Dairy J. , vol.43 , pp. 35-42
    • Zoon, P.1    Van Vliet, T.2    Walstra, P.3


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