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Enzymatic Coagulation of Milk

  • Chapter
Advanced Dairy Chemistry—1 Proteins

Abstract

The first step in the cheesemaking process involves the coagulation of milk. For the principal family of cheeses (75% of total cheese), this is achieved by adding a small amount of rennet or some other milk clotting enzyme or combination of enzymes to the milk; the alternative mechanism of coagulation is via acid (isoelectric) precipitation (see Chapter 22). Rennet is an extract from calfs’ stomach and contains as the clotting factor, calf chymosin. The term “rennet” is often used loosely to designate any particular milk clotting enzyme preparation.

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References

  • Alais, C. and Lagrange, A. (1972) Etude biochemique d’une protease coagulante produit par Mucor miehi. I. Active coagulante et activité proteolytique. Lait, 52, 407–27.

    Article  CAS  Google Scholar 

  • Armstrong, C.E., MacKinlay, A.G., Hill, R.J. and Wake, R.G. (1984) The action of rennin onκ-casein: the heterogenity and origin of the soluble product. Biochim. Biophys. Acta, 140, 123–31.

    Google Scholar 

  • Azuma, N., Kaminnnogawa, S. and Yamauchi, K. (1984) Properties of glyco-macropeptide and para-K-casein derived from humanκ-casein and comparison of human and bovineκ-casein as to susceptibility to chymosin and pepsin. Agr. Biol. Chem., 48, 2025–31.

    Article  CAS  Google Scholar 

  • Baki, M. and Wolfe, F.H. (1971) Destabilization of casein micelles by lysozyme. Can. J. Biochem., 49, 882–4.

    Article  Google Scholar 

  • Bauer, R., Hansen, M., Hansen, S., Ogendal, L., Lomholt, S.B., Qvist, K.B. and Home, D.S. (1995) 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, 2725–37.

    Article  CAS  Google Scholar 

  • Beeby, R. (1979) The proteolysis of casein by immobilized preparations of α-chymotrypsin, chymosin and a fungal protease. N.Z. J. Dairy Sci. Technol., 14, 1–11.

    CAS  Google Scholar 

  • Beeby, R. (1980) The use of fluorescamine at pH 6.0 to follow the action of chymosin onκ-casein and to estimate this protein in milk. N.Z. J. Dairy Sci. Technol., 15, 99–108.

    CAS  Google Scholar 

  • Berridge, N.J. (1942) The second phase of rennet coagulation. Nature, 149, 194–5.

    Article  CAS  Google Scholar 

  • Berridge, N.J. (1945) The purification and crystallization of rennin. Biochem. J., 39, 179–86.

    CAS  Google Scholar 

  • Bines, V., Young, P. and Law, J.A. (1989) Comparison of Cheddar cheese made with a recombinant calf chymosin with standard calf rennet. J. Dairy Res., 56, 657–64.

    Article  CAS  Google Scholar 

  • Bitri, L., Rolland, M.P. and Besancon, P. (1993) Immunological detection of bovine caseinomacropeptide in ovine and caprine dairy products. Milchwissenschaft, 48, 367–70.

    CAS  Google Scholar 

  • Bloomfield, V.A. and Morr, C.V. (1973) Structure of casein micelles: physical methods. Neth. Milk Dairy J., 27, 103–20.

    CAS  Google Scholar 

  • Bohak, Z. (1969) Purification and characterization of chicken pepsinogen and chicken pepsin. J. Biol. Chem., 244, 4638–48.

    CAS  Google Scholar 

  • Bringe, N.A. and Kinsella, J.E. (1986) Influence of calcium chloride on the chymosin-initiated coagulation of casein micelles. J. Dairy Res., 53, 371–9.

    Article  CAS  Google Scholar 

  • Burchard, W. (1978) Application of cascade theory to calculation of quasielastic scattering functions. I. Polydisperse, ideal, linear chains in dilute solution. Macromolecules, 11, 455–9.

    Article  CAS  Google Scholar 

  • Burchard, W., Schmidt, M. and Stockmayer, W.H. (1980) Information on poly-dispersity and branching from combined quasielastic and integrated scattering. Macromolecules, 13, 1265–72.

    Article  CAS  Google Scholar 

  • Carlson, A., Hill, G.C. and Olson, N.F. (1986) The coagulation of milk with immobilized enzymes: a critical review. Enz. Microb. Technol., 8, 642–50.

    Article  CAS  Google Scholar 

  • Castle, A.V. and Wheelock, J. (1972) Effect of varying enzyme concentration on the action of rennin on whole milk. J. Dairy Res., 39, 15–22.

    Article  CAS  Google Scholar 

  • Chaplin, B. and Green, M.L. (1980) Determination of the proportion ofκ-casein hydrolyzed by rennet on coagulation of skim milk. J. Dairy Res., 47, 351–8.

    Article  CAS  Google Scholar 

  • Culioli, J. and Sherman, P. (1978) Rheological aspects of the renneting of milk concentrated by ultrafiltration. J. Text. Studies, 9, 257–81.

    Article  CAS  Google Scholar 

  • Dalgleish, D.G. (1979) Proteolysis and aggregation of casein micelles treated with immobilized or soluble chymosin. J. Dairy Res., 46, 653–61.

    Article  CAS  Google Scholar 

  • Dalgleish, D.G. (1980a) Effect of milk concentration on the rennet coagulation time. J. Dairy Res., 47, 231–5.

    Article  CAS  Google Scholar 

  • Dalgleish, D.G. (1980b) A mechanism for the chymosin-induced flocculation of casein micelles. Biophys. Chem., 11, 147–55.

    Article  CAS  Google Scholar 

  • Dalgleish, D.G. (1981) Effect of milk concentration on the nature of curd formed during renneting — a theoretical discussion. J. Dairy Res., 48, 65–9.

    Article  CAS  Google Scholar 

  • Dalgleish, D.G., Brinkhuis, J. and Payens, T.A.J. (1981) The coagulation of differently sized casein micelles by rennet. Eur. J. Biochem., 119, 257–61.

    Article  CAS  Google Scholar 

  • Dalgleish, D.G. (1983) Coagulation of renneted casein micelles: dependence on temperature, calcium ion concentration and ionic strength. J. Dairy Res., 50, 331–40.

    Article  CAS  Google Scholar 

  • Dalgleish, D.G. (1984) Measurement of electrophoretic mobilities and zeta-potentials of particles from milk using laser doppler electrophoresis. J. Dairy Res., 51, 425–38.

    Article  CAS  Google Scholar 

  • Dalgleish, D.G. (1986) Analysis of fast protein liquid chromatography of variants of K-casein and their relevance to micellar structure and renneting. J. Dairy Res., 53, 43–51.

    Article  CAS  Google Scholar 

  • Dalgleish, D.G. (1988) A new calculation of the kinetics of the renneting reaction. J. Dairy Res., 55, 221–8.

    Google Scholar 

  • Dalgleish, D.G. (1989) The behavior of minerals in heated milks, Bulletin 238, International Dairy Federation, Brussels, pp. 31–4.

    Google Scholar 

  • Dalgleish, D.G. (1993) The enzymatic coagulation of milk, in Cheese: Chemistry, Physics and Microbiology, Vol. 2, (P.F. Fox ed.) Chapman and Hall, London, pp. 69–100.

    Chapter  Google Scholar 

  • Dalgleish, D.G. (1998) Casein micelles as colloids: surface structures and stabilities. J. Dairy Sci., 81, 3013–8.

    Article  CAS  Google Scholar 

  • Dalgleish, D.G. and Holt, C. (1988) A geometric model to describe the initial aggregation of partly renneted casein micelles. J. Colloid Interf. Sci., 123, 80–4.

    Article  CAS  Google Scholar 

  • Damiez, W. and Dziuba, J. (1975) Studies on casein proteolysis. I. Enzymatic phase of casein coagulation as influenced by heat treatment of milk proteins. Milchwissenschaft, 30, 399–105.

    Google Scholar 

  • Daniels, F. and Alberty, R.A. (1966) Physical Chemistry, 3rd edn, John Wiley, New York, pp. 360–2.

    Google Scholar 

  • Darling, D.F. and Dickson, J. (1979) The determination of the zeta potential of casein micelles. J. Dairy Res., 46, 329–32.

    Article  CAS  Google Scholar 

  • Darling, D.F. and van Hooydonk. A.C.M. (1981) Derivation of a mathematical model for the mechanism of casein micelle coagulation by rennet. J. Dairy Res., 48, 189–200.

    Article  CAS  Google Scholar 

  • de Koning, P.J. (1978) Coagulating enzymes in cheese making. Dairy Ind. Int., 43 (7), 7–13.

    Google Scholar 

  • de Kruif, C.G. and May, R.P. (1991) Structure, interaction and gelling studied by small-angle neutron scattering. J. Biochem., 200, 431–6.

    Google Scholar 

  • de Kruif, C.G. Jeurinik, T.J.M. and Zoon, P. (1992) The viscosity of milk during the initial stages of renneting. Neth. Milk Dairy J., 46, 123–37.

    Google Scholar 

  • de Kruif, C.G. (1998) Supra-aggregates of casein micelles as a prelude to coagulation. J. Dairy Sci., 81, 3019–28.

    Article  Google Scholar 

  • de Roos, A.L. (1999) The Adsorption of Lysozyme and Chymosin onto Emulsion Droplets and their Association with Caseins, Thesis, Agricultural University of Wageningen, Netherlands.

    Google Scholar 

  • de Roos, A.L., Walstra, P. and Guerts, T.J. (1995) Association of chymosin with adsorbed caseins, in Food Macromolecules and Colloids, (E. Dickinson and D. Lorient eds.) The Royal Society of Chemistry, Cambridge, pp. 50–7.

    Chapter  Google Scholar 

  • Dewan, R.A.J. and Bloomfield, V.A. (1972) Molecular weight of bovine milk casein micelles from diffusion and viscosity measurements. J. Dairy Sci., 56, 66–8.

    Article  Google Scholar 

  • Doty, P. and Steiner, R.F. (1950) Light scattering and spectrophotemetry of colloidal solutions. J. Chem. Phys., 18, 1211–20.

    Article  CAS  Google Scholar 

  • Drake, R.L. (1972) The scalar transport equation of coalescence theory: moments and kernals. J. Atm. Sci., 29, 537–47.

    Article  Google Scholar 

  • Dunnewind, B, de Roos, A.L. and Guerts, T.J. (1996) Association of chymosin with caseins in solution. Neth. Milk Dairy J., 50, 121–33.

    CAS  Google Scholar 

  • Ernstrom, C.A. (1974) Milk clotting enzymes and cheese chemistry, in Fundamentals of Dairy Chemistry, 2nd edn, (B.H. Webb, A.H. Johnson and J.A. Alford eds.) AVI Publishing Co, Inc., Westport, CT, pp. 694–700.

    Google Scholar 

  • Farrell, H.M., Jr., Brown, E.M. and Kumosinski, T.F. (1993) Three-dimensional molecular modeling of bovine caseins. Food Structure, 12, 235–50.

    CAS  Google Scholar 

  • Farrell, H.M., Wickham, E.D. and Groves, M.L. (1998) Environmental influences on purifiedκ-casein: disulfide interactions. J. Dairy Sci., 81, 2974–84.

    Article  CAS  Google Scholar 

  • Foltmann, B. (1971) The biochemistry of prorennin (prochymosin) and rennin (chymosin), in Milk Proteins; Chemistry and Molecular Biology, Vol. 2, (H.A. McKenzie ed.) Academic Press, New York, pp. 218–21.

    Google Scholar 

  • Foltmann, B. (1993) General and molecular aspects of rennets, in Cheese: Chemistry, Physics and Microbiology, Vol. 2, 2nd edn. (P.F. Fox ed.) Chapman and Hall, London, pp. 37–68.

    Chapter  Google Scholar 

  • Fox, K.K., Holsinger, V.H., Polsati, L.P. and Pallansch, M.J. (1967) Separation of β-lactoglobulin from other milk serum protein by trichloroacetic acid. J. Dairy Sci., 50, 1363–7.

    Article  CAS  Google Scholar 

  • Fox, P.F. (1969) Milk — clotting and proteolytic activities of rennet, and of bovine pepsin and porcine pepsin. J. Dairy Res., 36, 427–33.

    Article  CAS  Google Scholar 

  • Fox, P.F. (1981) Heat-induced changes in milk preceding coagulation. J. Dairy Sci., 6, 2127–37.

    Article  Google Scholar 

  • Fox, P.F. and Morrissey, P.A. (1972) Casein micelle structure: location ofκ-casein. J. Dairy Res., 39, 387–94.

    Article  CAS  Google Scholar 

  • Gamier, J. (1963) Etude cinetique d’une protolyse limitee: action de la pressure sur la casein K. Biochim. Biophys. Acta, 66, 366–77.

    Article  Google Scholar 

  • Garnier, J., Mocquot, G., Ribadeau-Dumas, B. and Maubois, J.-L. (1968) Coagulation du lait par la pressure: aspects scientifiques et technologiques. Ann. Nutr. Alim., 22, B495–552.

    CAS  Google Scholar 

  • Garnot, P. and Corre, C. (1980) Influence of milk protein concentration on the gelling activity of chymosin and bovine pepsin. J. Dairy Res., 47, 103–11.

    Article  CAS  Google Scholar 

  • Garnot, P., Rank, T.C. and Olson, N.F. (1982) Influence of protein and fat contents on ultrafiltrated milk and rheological properties of gels formed by chymosin. J. Dairy Sci., 65, 2267–73.

    Article  CAS  Google Scholar 

  • Gatt, S. and Bartfai, T. (1977) Rate equations and simulation curves for enzymatic reactions which utilize lipids as substrates, II. Effect of adsorption of the substrate or enzyme on the steady-state kinetics. Biochim. Biophys. Acta, 488, 13–24.

    Article  CAS  Google Scholar 

  • Gibbons, R.A. and Cheeseman, G.C. (1962) Action of rennin on casein: The function of neuraminic acid residues. Biochim. Biophys. Acta, 56, 354–56.

    Article  CAS  Google Scholar 

  • Gillialand, G.L., Oliva, M.T. and Dill, J. (1991) Functional implications of the three dimension structure of bovine chymosin, in Structure and Function of Aspartic Proteinases. Genetics, Structures and Mechanisms, (B.M. Dunn ed.) Plenum Press, New York, pp. 23–37.

    Chapter  Google Scholar 

  • Glatter, D., Hofer, M., Jorde, C. and Eigner, W.D. (1985) Interpretation of elastic light-scattering data in real space. J. Colloid Interf. Sci., 105, 577–86.

    Article  CAS  Google Scholar 

  • Green, M.L. and Crutchfield, G. (1971) Density gradient electrophoresis of nature and rennet-treated casein micelles. J. Dairy Res., 38, 151–64.

    Article  CAS  Google Scholar 

  • Green, M.L. and Foster, P.M.D. (1974) Comparison of the rates of proteolysis during ripening of Cheddar cheeses made with calf and swine pepsin as coagulants. J. Dairy Res., 41, 269–82.

    Article  CAS  Google Scholar 

  • Green, M.L. and Marshall, R.F. (1977) The acceleration by cationic materials of the coagulation of casein micelles by rennet. J. Dairy Res., 44, 521–31.

    Article  CAS  Google Scholar 

  • Green, M.L., Hobbs, D.G., Morant, S.V. and Hill, V.A. (1978) Intermicellar relationships in rennet treated separated milk. II. Process of gel assembly. J. Dairy Res., 45, 413–22.

    Article  CAS  Google Scholar 

  • Green, M.L. and Morant, S.V. (1981) Mechanism of aggregation of casein micelles in rennet-treated milk. J. Dairy Res., 48, 57–63.

    Article  CAS  Google Scholar 

  • Guthy, K. and Novak, G. (1977) Observations on the primary phase of milk coagulation by rennet under standardized conditions. J. Dairy Res., 44, 363–6.

    Article  CAS  Google Scholar 

  • Hamdy, A. and Edelstein, D. (1970) Some factors affecting the coagulation strength of three different microbial rennets. Milchwissenschaft, 25, 450–3.

    CAS  Google Scholar 

  • Hicks, C.L., O’Leary, J. and Bucy, J. (1988) Use of recombinant chymosin in the manufacture of Cheddar and Colby cheese. J. Dairy Sci.. 71, 1127–31.

    Article  CAS  Google Scholar 

  • Hiemenz, P.C. (1986) Principles of Colloid and Surface Chemistry, 2nd edn, Marcel Dekker, New York, pp. 223–86.

    Google Scholar 

  • Hill, R.J. and Wake, R.G. (1969) Amphiphile nature ofκ-casein as the basis for its micelle stabilizing property. Nature, 221, 635–9.

    Article  CAS  Google Scholar 

  • Hindle, E.J. and Wheelock, J.V. (1970) The primary phase of rennin action in heat stabilized milk. J. Dairy Res., 37, 389–96.

    Article  CAS  Google Scholar 

  • Holmes, D.G., Duersch, J.W. and Ernstrom, G.A. (1977) Distribution of milk — clotting enzymes between curd and whey and their survival during Cheddar cheesemaking. J. Dairy Sci., 60, 862–9.

    Article  CAS  Google Scholar 

  • Holt, C. (1985) The size distribution of bovine casein micelles: a review. Food Microstructure, 4, 1–10.

    CAS  Google Scholar 

  • Holt, C. and Dalgleish, D.G. (1986) Electrophoretic and hydrodynamic properties of bovine casein micelle interpreted in terms of particles with an outer hairy layer. J. Colloid Interf. Sci., 114, 513–24.

    Article  CAS  Google Scholar 

  • Holt, C. and Home, D.S. (1996) The hairy casein micelles: evolution of the concept and its implication for dairy technology. Neth. Milk Dairy J., 50, 85–111.

    CAS  Google Scholar 

  • Holter, H. (1932) Uber die labwirkung. Biochem. Z., 255, 160–88.

    CAS  Google Scholar 

  • Home, D.S. (1984) Steric effects in the coagulation of casein micelles by ethanol. Biopolymers, 23, 989–93.

    Article  Google Scholar 

  • Home, D.S. (1987) Determination of the fractal dimension using turbidimetric techniques. Faraday Disc. Chem. Soc., 83, 259–70.

    Article  Google Scholar 

  • Home, D.S. and Davidson, C.M. (1993) Direct observation of decrease in size of casein micelles during the initial stages of renneting of skim milk. Int. Dairy J., 3, 61–71.

    Article  Google Scholar 

  • Humbert, G., Driou, A., Guerin, J. and Alais, C. (1980) Effect of high pressure homogenzation on the properties of milk and its enzyme clotting characteristics. Lait, 60, 574–94.

    Article  CAS  Google Scholar 

  • Humme, H.E. (1972) The optimum pH for the limited specific proteolysis ofκ-casein by rennin (primary phase of milk clotting). Neth. Milk Dairy J., 26, 180–5.

    CAS  Google Scholar 

  • Humphrey, R.S. and Newsome, L.J. (1984) High performance ion-exchange chromatography of the major bovine milk proteins. N.Z. J. Dairy Sci. Technol., 19, 197–204.

    CAS  Google Scholar 

  • Hyldig, G. (1993) Effect of Technological Factors on the Enzymatic Reaction and Gel Formation in Milk and Ultrafiltration Concentrates, Thesis, The Royal Veterinary and Agricultural University, Copenhagen, Denmark.

    Google Scholar 

  • Hylsop, D.B. (1989) Enzymatically initiated coagulation of casein micelles: a kinetic model. Neth. Milk Dairy J., 43, 163–70.

    Google Scholar 

  • Hyslop, D.B. (1993) Enzyme-induced coagulation of casein micelles: a number of different kinetic models. J. Dairy Res., 60, 517–33.

    Article  CAS  Google Scholar 

  • Hyslop, D.B. and Qvist, K.B. (1996) Application of numerical analysis to a number of models for chymosin-induced coagulation of casein micelles. J. Dairy Res., 63, 223–32.

    Article  CAS  Google Scholar 

  • Hyslop, D.B., Swanson. A.M. and Lund, D.B. (1979) Heat inactivation of milkclotting enzymes at different pH. J. Dairy Sci., 62, 1227–32.

    Article  CAS  Google Scholar 

  • Jakob, E. and Puhan, Z. (1992) Technological properties of milk as influenced by genetic polymorphism of milk proteins-a review. Int. Dairy J., 2, 157–78.

    Article  CAS  Google Scholar 

  • Kannan, A. and Jenness, R. (1961) Relation of milk serum proteins and milk salts to the effects of heat treatment clotting. J. Dairy Sci., 44, 808–22.

    Article  CAS  Google Scholar 

  • Kumosinski, T.F. Brown, E.M. and Farrell, H.M., Jr. (1991) Three-dimensional molecular modelling of bovine caseins:κ-casein. J. Dairy Sci., 74, 2879–87.

    Article  CAS  Google Scholar 

  • Kumosinski, T.F., Brown, E.M. and Farrell, H.M., Jr. (1993) Three-dimensional molecular modeling of bovine caseins: a refined, energy minimizedκ-casein structure. J. Dairy Sci., 76, 2507–20.

    Article  CAS  Google Scholar 

  • Lagrange, A., Paquit, P.D. and Alais, C. (1980) Comparative study of two Mucor miehei acid proteinases. Purification and some molecular properties. Int. J. Biochem., 11, 347–52.

    Article  CAS  Google Scholar 

  • Lomholt, S.B. and Qvist, K.B. (1997) Relationship between rheological properties and degree ofκ-casein proteolysis during renneting of milk. J. Dairy Res., 64, 541–9.

    Article  CAS  Google Scholar 

  • Lomholt, S.B., Worning, P., Ogendal, L., Qvist, K.B., Hyslop, D.B. and Bauer, R. (1998) Kinetics of the renneting reaction followed by measurement of turbidity as a function of wavelength. J. Dairy Res., 65, 545–54.

    Article  CAS  Google Scholar 

  • Martin, P., Raymond, M.N., Bricas, E. and Ribadeau Dumas, B. (1980) Kinetic studies on the action of Mucor pusillus, Mucor miehei acid proteinases and chymosins A and B on synthetic chromophoric hexapeptide. Biochim. Biophys. Acta, 612, 410–20.

    Article  CAS  Google Scholar 

  • McMahon, D.J. and Brown, R.J. (1984) Enzymatic coagulation of casein micelles: a review. J. Dairy Sci., 67, 919–29.

    Article  CAS  Google Scholar 

  • McMahon, D.J. and McManus, W.R. (1998) Rethinking casein micelle structure using electron microscopy. J. Dairy Sci., 81, 2985–93.

    Article  CAS  Google Scholar 

  • Mehai, M.A. and Cheryan, M. (1983a) The secondary phase of milk coagulation. Effect of calcium, pH and temperature on clotting activity. Milchwissenschft, 38, 137–40.

    Google Scholar 

  • Mehai, M.A. and Cheryan, M. (1983b) Coagulation studies of ultrafiltraion — concentrated skin milk. Milchwissenschaft, 38, 708–10.

    Google Scholar 

  • Morrissey, P.A. (1969) The rennet hysteresis of heated milk. J. Dairy Res., 36, 333–41.

    Article  CAS  Google Scholar 

  • Mulder, H. and Walstra, P. (1974) The Milk Fat Globule. Emulsion Science as Applied to Milk Products and Comparable Foods, Commonwealth Agricultural Bureau, Farnham Royal, UK.

    Google Scholar 

  • Napper, D.H. (1983) Polymeric Stabilization of Colloidal Dispersions. Academic Press, London, pp. 197–215.

    Google Scholar 

  • Oortwijn, H., Walstra, P. and Malder, H. (1977) The membranes of recombined fat globules. I. Electron microscopy. Neth. Milk Dairy J., 31, 134–47.

    Google Scholar 

  • Oortwijn, H. and Walstra, P. (1979) The membranes of recombined fat globules. II. Composition. Neth. Milk Dairy J., 33, 134–54.

    CAS  Google Scholar 

  • Overbeek, J.T.G. (1952) Kinetics of flocculation, in Colloid Science, Vol. 1, (H.R. Kruyt ed.) Elsevier, Amsterdam, pp. 278–323.

    Google Scholar 

  • Paquet, P.D. and Alais, C. (1978) Action de proteases foniqiques sur la casein bovine et ses constituants. Milchwissenschqft, 33, 87–90.

    CAS  Google Scholar 

  • Payens, T.A.J. (1976) On the enzyme — triggered clotting of casein; a preliminary account. Neth. Milk Dairy J., 30, 55–9.

    CAS  Google Scholar 

  • Payens, T.A.J., Wiersma, A.K. and Brinkhuis, J. (1977) On enzymatic clotting processes. I. Kinetics of enzyme triggered coagulation reactions. Biophys. Chem., 6, 253–61.

    Article  CAS  Google Scholar 

  • Payens, T.A.J. (1977) On enzymatic clotting processes, II. The colloidal instability of chymosin-treated casein micelles. Biophys. Chem., 6, 263–70.

    Article  CAS  Google Scholar 

  • Payens, T.A.J. (1979) Casein micelles: The colloidal chemical approach. J. Dairy Res., 46, 291–306.

    Article  CAS  Google Scholar 

  • Payens, T.A.J. and Both, P. (1980) On enzymatic coagulation processes. IV. The chymosin-triggered clotting of para-κ-casein, in Bioelectrochemistry: Ions, Surfaces, Membranes. (M. Blank ed.) Adv. Chem. Series No 188 American Chemical Society, Washington, DC, pp. 129–41.

    Chapter  Google Scholar 

  • Payens, T.A.J. and Visser. S. (1981) What determines the specificity of chymosin towardsκ-casein? Neth. Milk Dairy J., 35, 387–9.

    CAS  Google Scholar 

  • Payens, T.A.J. (1984) The relationship between milk concentration and rennet coagulation time. J. Appl. Biochem., 6, 22–239.

    Google Scholar 

  • Payens, T.A.J. and Brinkhuis, J. (1986) Mean field kinetics of the enzyme — triggered gelation of casein micelles. Colloid. Surf., 20, 37–50.

    Article  CAS  Google Scholar 

  • Payens, T.A.J. (1989) The enzyme triggered coagulation of casein micelles. Adv. Colloid Interf. Sci., 30, 31–69.

    Article  CAS  Google Scholar 

  • Pearse, K.N. (1976) Moving boundry electrophoresis of native and rennet-treated casein micelles. J. Dairy Res., 43, 27–36.

    Article  Google Scholar 

  • Pearse, M.J., Linklater, P.M., Holl, R.J. and MacKinlay, A.G. (1985) Effect of heat induced interaction between β-lactoglobulin andκ-casein on syneresis. J. Dairy Res., 52, 159–65.

    Article  CAS  Google Scholar 

  • Picard, C., Plard, I., Rondaux — Gaida, D. and Collin, J.-C. (1994) Detection of proteolysis in raw milk stored at low temperature by inhibition ELISA. J. Dairy Res., 61, 395–404.

    Article  CAS  Google Scholar 

  • Plowman, J.E. and Creamer, L.K. (1995) Restrained molecular dynamics study of the interaction between bovineκ-casein peptide 98-111 and bovine chymosin and porcine pepsin. J. Dairy Res., 62, 451–67.

    Article  CAS  Google Scholar 

  • Prin, C., El Bari, N., Montagne, P., Cuilliere, M-C,B., Faure, G., Humbert, G. and Linden, G. (1996) Microparticle — enhanced nephelometric immunoassay for caseinomacropeptide in milk. J. Dairy Res., 63, 73–81.

    Article  CAS  Google Scholar 

  • Pujolle, J., Ribadeau Dumas. B., Gamier, J. and Pion, R. (1966) A study ofκ-casein components. I. Preparation. Evidence of a common C-terminal sequence. Biochem. Biophys. Res. Comm., 25, 285–90.

    Article  CAS  Google Scholar 

  • Qvist, K.B. (1979a) Reestablishment of the original rennetability of milk after cooling. I. The effect of cooling and LTST pasteurization of milk and renneting. Milchwissenschaft, 34, 467–9.

    Google Scholar 

  • Qvist, K.B. (1979b) Reestablishment of the original rennetability of milk after cooling, II. The effect of some additives. Milchwissenschaft, 34, 600–3.

    CAS  Google Scholar 

  • Raap, J., Kerling, H.J., Vreeman. H.J. and Visser, S. (1983) Peptide substrates for chymosin (rennin): conformational studies ofκ-casein andκ-casein-related oligopeptides by circular dichroism and secondary structure prediction. Arch. Biochem. Biophys., 221, 117–24.

    Article  CAS  Google Scholar 

  • Rasmussen, L.K., Hojrup, P. and Petersen, T.E. (1992) The multimeric structure and disulfide — boning pattern of bovineκ-casein. Eur. J. Biochem., 207, 215–22.

    Article  CAS  Google Scholar 

  • Reddy, I.M. and Kinsella, J.E. (1990) Interaction of β-lactoglobulin withκ-casein in micelles as assessed by chymosin hydrolysis: effect of temperature, heating time, β-lactoglobulin concentration and pH. J. Agr. Food Chem., 38, 50–8.

    Article  CAS  Google Scholar 

  • Reuter, H., Hisserich, D. and Prokopek, D. (1981) Beitragzus formalkinetic der labqerinnung von durch Ultrafiltration konzentrierter milch. Milchwissenschaft, 36, 13–8.

    CAS  Google Scholar 

  • Robson, E.W. and Dalgleish, D.G. (1984) Coagulation of homogenized milk particles by rennet. J. Dairy Res., 51, 417–24.

    Article  Google Scholar 

  • Roefs, S.P.F.M., Walstra, P., Dalgleish, D.G. and Home, D.S. (1985) Preliminary note on the change in casein micelles caused by acidification. Neth. Milk Dairy J., 39, 119–22.

    CAS  Google Scholar 

  • Ruettimann, K.W. and Ladish, M.R. (1991) In situ observation of casein micelle coagulation. J. Colloid Interf. Sci., 146, 276–87.

    Article  CAS  Google Scholar 

  • Saputra, D., Payne, F.A. and Hicks, G.L. (1994) Analysis of enzymatic hydrolysis of K-casein in milk using diffuse reflectance near-infrared radiation. Trans. ASAE, 37, 1947–55.

    CAS  Google Scholar 

  • Sawyer, W.H. (1969) Complex between β-lactoglobulin andκ-casein. A review. J. Dairy Sci., 52, 1347–55.

    Article  CAS  Google Scholar 

  • Schmidt, D.G. (1982) Association of caseins and casein micelle structure, in Developments in Dairy Chemistry. Vol. 1, (P.F. Fox ed.) Applied Science, London, pp. 61–86.

    Google Scholar 

  • Schmidt, D.G., Both, P. and de Koning, P.J. (1966) Fractionation of some properties of kappa-casein variants. J. Dairy Sci., 49, 776–82.

    Article  CAS  Google Scholar 

  • Schmidt, M., Dittman, N. and Burchard, W. (1978) Quasi-elastic light scattering from branched polymers: I. Polyvinyl acetate and polyvinyl acetate-microgels prepared by emulsion polymerization. Polymer, 20, 582–8.

    Article  Google Scholar 

  • Scott-Blair, G.W. and Oosthuizen, J.C., (1961) A viscometric study of the breakdown of casein in milk by rennin and rennet. J. Dairy Res., 28, 165–73.

    Article  Google Scholar 

  • Shammet, K.M., Brown, R.J. and McMahon, D.J., (1992) Proteolytic activity of some milk-clotting enzymes onκ-casein. J. Dairy Sci., 75, 1373–9.

    Article  CAS  Google Scholar 

  • Slattery, C.W. and Evard, R., (1973) A model for the formation and structure of casein micelles from subunits of variable composition. Biochim. Biophys. Acta, 317, 529–38.

    Article  CAS  Google Scholar 

  • Smits, P. and van Brouwershaven, J.H. (1980) Heat-induced association of β-lactoglobulin and casein micelles. J. Dairy Res., 47, 313–25.

    Article  CAS  Google Scholar 

  • Soxhlet, F. (1877a) Die darftelung halt baren labtliiffigteiten. Milch. Z., 37, 495–501.

    Google Scholar 

  • Soxhlet, F. (1877b) Die darftellung halt baren labtliiffigteiten. Milch. Z., 38, 513–4.

    Google Scholar 

  • Stockmayer, W.H. (1943) Theory of molecular size distribution and gel formation in branched chain polymers. J. Chem. Phys., 11, 45–55.

    Article  CAS  Google Scholar 

  • Sutherland, D.N. (1970) Chain formation of fine particle aggregates. Nature, 226, 1241–2.

    Article  CAS  Google Scholar 

  • Tadros, T.F. (1984) Suspensions, in Surfactants, (T.F. Tadros ed.) Academic Press, London, pp. 197–220.

    Google Scholar 

  • Tarn, J.J. and Whitaker, J.R. (1972) Rates and extents of hydrolysis of several caseins by pepsin, rennin, Endothia parasitica proteinase and Mucor pusillus proteinase. J. Dairy Sci., 55, 1523–31.

    Article  Google Scholar 

  • Thunell, R.K., Duersch, J.W. and Ernstrom, C.A. (1979) Thermal inactivation of residual milk-clotting enzymes in whey. J. Dairy Sci., 62, 373–7.

    Article  CAS  Google Scholar 

  • Thurn, A., Blanchard, W. and Niki, R. (1987) Structure of casein micelles. I. Small angle neutron scattering from β-andκ-casein. Colloid Polym. Sci., 265, 653–66.

    Article  CAS  Google Scholar 

  • Undenfriend, S., Stein, S., Bohlen, P., Dairman, W., Leimgruber, W. and Weigele, M. (1972) Fluorescamine: a reagent for assay of amino acids, peptides, proteins and primary amines in the picomole range. Science, 178, 871–2.

    Article  Google Scholar 

  • van Holde, K.E. (1971) Physical Biochemistry. Prentice Hall, London, pp. 180–201.

    Google Scholar 

  • van Hooydonk, A.C.M. and Olieman, C. (1982) A rapid and sensitive high-performance liquid chromatography method following the action of chymosin on milk. Neth. Milk Dairy J., 36, 153–8.

    Google Scholar 

  • van Hooydonk, A.C.M., Olieman, C. and Hagedoorn, H.G. (1984) Kinetics of the chymosin-catalyzed proteolysis ofκ-casein in milk. Neth. Milk Dairy J., 38, 207–22.

    Google Scholar 

  • van Hooydonk, A.C.M., Hagedoorn, H.G. and Boerringter, I.J. (1986a) pH-induced physico-chemical changes of casein micelles in milk and their effect on renneting. I. Effect of acidification on physico-chemical properties. Neth. Milk Dairy J., 40, 281–96.

    Google Scholar 

  • van Hooydonk, A.C.M., Hagedoorn, H.G. and Boerringter, I.J. (1986b) pH-induced physico-chemical changes of casein micelles in milk and their effect on renneting. II. Effect of pH on renneting of milk. Neth. Milk Dairy J., 40, 297–313.

    Google Scholar 

  • van Hooydonk, A.C.M., Hagedoorn, H.G. and Boerringter, I.J. (1986c) The effect of various cations on the renneting of milk. Neth. Milk Dairy J., 40, 369–90.

    Google Scholar 

  • van Hooydonk, A.C.M. and Walstra, P. (1987) Interpretation of the kinetics of the renneting reaction in milk. Neth. Milk Dairy J., 41, 19–47.

    Google Scholar 

  • van Hooydonk, A.C.M., de Koster. P.G. and Boerringter, I.J. (1987) The renneting properties of heated milk. Neth. Milk Dairy J., 41, 3–18.

    Google Scholar 

  • van Kreveld, A. and van Minnen, G. (1995) Calcium and magnesium ion activity in raw milk and processed milk. Neth. Milk Dairy J., 9, 1–29.

    Google Scholar 

  • Verger, R., Mieras, M.C.E. and de Hass, H.G., (1973) Action of phospholipase A at interfaces. J. Biol. Chem., 248, 4024–34.

    Google Scholar 

  • Visser, S., Van Rooijen, P.J., Schattenlzerk, C. and Kerling, K.E.T. (1976) Peptide substrates for chymosin (rennin). Kinetic studies with peptides of different chain length including parts of the sequence 101-112 of bovineκ-casein. Biochim. Biophys. Acta, 438, 265–72.

    Article  CAS  Google Scholar 

  • Visser, S., van Rooijen, P.J. and Slangen, C.J. (1980) Peptide substrates for chymosin (rennin). Isolation and substrate behavior of two tryptic fragments of bovine K-casein. Eur. J. Biochem., 108, 415–421.

    Article  CAS  Google Scholar 

  • Visser, S. (1981) Proteolytic enzymes and their action on milk proteins. A review. Neth. Milk Dairy J., 35, 65–88.

    CAS  Google Scholar 

  • Visser, S., Slangen, C.J. and van Rooijen, P.J. (1987) Interaction sites inκ-casein-related sequence located outside the (103-108)-hexapeptide region that fits into the enzyme’s active-site cleft. Biochem. J., 244, 553–8.

    CAS  Google Scholar 

  • Vreeman, H.J., Brinkhuis, J.A. and van der Spek, C.A. (1981) Some association properties of bovine SH-K-casein. Biophys. Chem., 14, 185–93.

    Article  CAS  Google Scholar 

  • Vreeman, H.J., Visser, S., Slanger, C.J. and van Riel, A. (1986) Characterization of bovineκ-casein fractions and kinetics of chymosin-induced macropeptide release from carbohydrate-free and carbohydrate-containing fractions determined by high-performance gel-permeation chromatography. Biochem. J., 240, 87–97.

    CAS  Google Scholar 

  • Walstra, P. (1979) The voluminosity of bovine casein micelles and some of its implications. J. Dairy Res., 46, 317–23.

    Article  CAS  Google Scholar 

  • Walstra, P., Bloomfield, V.A., Wei. G.J. and Jenness, R. (1981) Effect of chymosin on the hydrodynamic diameter of casein micelles. Biochim. Biophys. Acta, 669, 258–9.

    Article  CAS  Google Scholar 

  • Walstra, P. (1990) On the stability of casein micelles. J. Dairy Sci., 73, 1965–79.

    Article  CAS  Google Scholar 

  • Waugh, D.F. (1958) The interactions of αs1-, β-andκ-caseins in micelle formation, Disc. Faraday Soc., 25, 186–96.

    Article  Google Scholar 

  • Waugh, D.F. (1971) Formation and structure of casein micelles, in Milk Proteins. Chemistry and Molecular Biology, Vol. 2, (H.A. McKenzie ed.) Academic Press, New York, pp. 3–85.

    Google Scholar 

  • Wheelock, J.V. and Kirk, A. (1974) The role of β-lactoglobulin in the primary phase of rennin action on heated casein micelles and heated milk. J. Dairy Res., 41, 367–72.

    Article  CAS  Google Scholar 

  • Wilson, G.A. and Wheelock, J.V. (1972) Factors affecting the action of rennin in heated milk. J. Dairy Res., 39, 413–9.

    Article  CAS  Google Scholar 

  • Worning, P., Bauer, R., Ogendal, L. and Lomholt, S.B. (1998) A novel approach to turbidity of dense systems: an investigation of the enzymatic gelation of casein micelles. J. Colloid Interf. Sci., 203, 265–77.

    Article  CAS  Google Scholar 

  • Zittle, C.A. Thompson, M.P., Custer, J.H. and Cerbulis, J. (1962) κ-Casein-β-lactoglobulin interaction in solution when heated. J. Dairy Sci., 45, 807–10.

    Article  CAS  Google Scholar 

  • Zollikofer, E. (1949) Influence of homogenization on the rennet coagulation time of milk. Proc. XII Int. Dairy Congr. (Stockholm) Vol. 3, pp. 129–31.

    CAS  Google Scholar 

  • Zoon, P.T., van Vliet, T. and Walstra, P. (1988) Rheological properties of rennet-induced skim milk gels. II. The effect of temperature. Neth. Milk Dairy J., 42, 271–94.

    CAS  Google Scholar 

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Hyslop, D.B. (2003). Enzymatic Coagulation of Milk. In: Fox, P.F., McSweeney, P.L.H. (eds) Advanced Dairy Chemistry—1 Proteins. Springer, Boston, MA. https://doi.org/10.1007/978-1-4419-8602-3_24

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