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Effects of cations and anions on the rate of the acidic coagulation of casein micelles: the possible roles of different forces

Published online by Cambridge University Press:  01 June 2009

Neal A. Bringe  and
John E. Kinsella
Neal A. Bringe
Affiliation:
Institute of Food Science, Cornell University, Ithaca, NY 14853, USA
John E. Kinsella
Affiliation:
Institute of Food Science, Cornell University, Ithaca, NY 14853, USA
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Summary

Raw skim milk was diluted 1000-fold using distilled water or various salt solutions as specified. Smooth, hyperbolic profiles of coagulation rate v. pH for casein were calculated from recordings of turbidity (400 nm) with time. The effects of pH, cation type, anion type and cleavage of k−casein by chymosin (EC 3.4.23.4) were determined. The maximum of pH-coagulation rate profiles decreased by 63, 85 and 94% when the skim milk diluent was changed from water to salt solutions of NaCl (100 mM), CaCl2 (50 mM) or MgCl2 (50 mM). The maximum of the pH–coagulation rate profile was 15 times greater when the Ca salt was changed from CaCl2 to Ca(SCN)2 (50 mM). The highest pH at which casein coagulation occurred increased from 4·45 to > 6·0 when Cu2+ (1 mM) was included with casein micelles dispersed in CaCl2 solution (50 mM). The addition of chymosin to casein micelles suspended in CaCl2 solution (70 mM) eliminated the inhibition of casein coagulation by Ca2+ at pH 4·5. It is proposed that ions such as Mg2+, Ca2+, and Na+, which generally associate with casein phosphate and carboxylate groups, increased the H+ concentration required to initiate the coagulation of casein, because H+ must displace bound Ca2+, Mg2+ or Na+ to reduce repulsive hydration forces between casein micelles, allowing attractive hydration forces (e.g. hydrophobic phenomena) to cause casein coagulation. Furthermore, it is proposed that ions such as Cl−, Br−, and SCN− bind to lysine, arginine and histidine groups and thereby decrease repulsive hydration forces between cationic casein micelles.

Type
Original Articles
Information
Journal of Dairy Research , Volume 58 , Issue 2 , May 1991 , pp. 195 - 209
Copyright
Copyright © Proprietors of Journal of Dairy Research 1991

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References

REFERENCES

Berridge, N. J. 1942 The second phase of rennet coagulation. Nature, 149 194–195Google Scholar
Bingham, E. W. 1971 Influence of temperature and pH on the solubility of αsl-, β- and κ-casein. Journal of Dairy Science 54 1077–1080Google Scholar
Bringe, N. A. 1988 The mechanism of the acidic coagulation of casein micelles. PhD Thesis. Cornell University.Google Scholar
Bringe, N. A. & Kinsella, J. E. 1986 Influence of calcium chloride on the chymosin-initiated coagulation of casein micelles. Journal of Dairy Research 53 371–379Google Scholar
Bringe, N. A. & Kinsella, J. E. 1990 Acidic coagulation of casein micelles: mechanisms inferred from spectrophotometric studies. Journal of Dairy Research 57 365–375Google Scholar
Brinkhuis, J. & Payens, T. A. 1984 The influence of temperature on the flocculation rate of renneted casein micelles. Biophysical Chemistry 19 75–81Google Scholar
Brulé, G. & Lenoir, J. 1986 The coagulation of milk. In Cheesemaking: science and technology p. 13 (Ed. Eck, A.). New York: Lavoisier Publishing Inc.Google Scholar
Cann, J. R. & Phelps, R. A. 1955 Binding of salt ions by bovine γ-pseudoglobulin. Journal of American Chemical Society 77 4266–4270Google Scholar
Carr, C. W. 1953 Studies on the binding of small ions in protein solutions with the use of membrane electrodes. IV. The binding of calcium ions in solutions of various proteins. Archives of Biochemistry and Biophysics 46 424–431Google Scholar
Dalgleish, D. G. 1983 Coagulation of renneted bovine casein micelles: dependence on temperature, calcium ion concentration and ionic strength. Journal of Dairy Research 50 331–340Google Scholar
Dalgleish, D. G., Paterson, E. & Horne, D. S. 1981 Kinetics of aggregation of αs1-casein/Ca2+ mixtures: charge and temperature effects. Biophysical Chemistry 13 307–314.Google Scholar
Darling, D. F. 1982 The effect of environmental conditions on the steric stabilisation of casein micelles in milk. In The Effect of Polymers on Dispersion Properties pp. 285–300 (Ed. Tadros, Th. F.). London: Academic PressGoogle Scholar
Darling, D. F. & Dickson, J. 1979 Electrophoretic mobility of casein micelles. Journal of Dairy Research 46 441–451Google Scholar
Darling, D. F. & Van Hooydonk, A. C. M. 1981 Derivation of a mathematical model for the mechanism of casein micelle coagulation by rennet. Journal of Dairy Research 48 189–200Google Scholar
Davies, D. T. & Law, A. J. R. 1980 The content and composition of protein in creamery milks in south-west Scotland. Journal of Dairy Research 47 83–90Google Scholar
Delben, F. & Paoletti, S. 1974 Thermodynamics of polycarboxylate aqueous solutions. II. Dilatometry and calorimetry of nickel and barium binding. Journal of Physical Chemistry 78 1486–1490Google Scholar
Dickinson, F. & Stainsby, G. 1982 Colloidal aspects of milk—a case study. Colloids in Food pp. 411–461. London: Applied Science PublishersGoogle Scholar
Dickson, I. R. & Perkins, D. J. 1971 Studies on the interactions between purified bovine caseins and alkaline-earth metal ions. Biochemical Journal 124 235–240Google Scholar
Ehsani, R., Bennasar, M. & Tarodo De La Fuente, B. 1982 [Effect of cold acidification of milk before drying on the coagulation ability of reconstituted products.] Lait 62 276–300Google Scholar
Fless, H. A. & Klotz, I. M. 1956 The thermodynamics of metallo-protein combinations. Comparison of copper complexes with natural proteins. Journal of the American Chemical Society 74 887Google Scholar
Feitknecht, U., Gál, S. & Signer, R. 1963 [The binding of some alkali salts by casein.] Helvetica Chimica Acta 46 813–815Google Scholar
Fox, C. W. & Ernstrom, C. A. 1969 Role of calcium in the low-temperature acidification of skimmilk and the formation of direct-acid curd. Journal of Dairy Science 52 885Google Scholar
Fox, S. W. & Foster, J. F. 1957 Introduction to Protein Chemistry pp. 241. New York: WileyGoogle Scholar
Fridovich, I. 1963 Inhibition of acetoacetic decarboxylase by anions. Journal of Biological Chemistry 238 592–598CrossRefGoogle ScholarPubMed
Gekko, K., Mugishima, H. & Koga, S. 1987 Effects of sugars and polyols on the sol-gel transition of κ-carrageenan: calorimetric study. International Journal of Biological Macromolecules 9 146Google Scholar
Griffin, M. C. A. 1987 Structural studies of casein micelles using photon correlation spectroscopy. Journal of Colloid and Interface Science 115 499–506CrossRefGoogle Scholar
Griffin, M. C. A. 1990 Steric stabilization and flow properties of concentrated casein micellar suspensions. In Food Colloids p. 110 (Eds Bee, R. D., Richmond, P. and Mingins, J.). Colworth, UK: Royal Society of ChemistryGoogle Scholar
Griffin, M. C. A., Price, J. C. & Martin, S. R. 1986 Effect of alcohols on the structure of caseins: circular dichroism studies of κ-casein A. International Journal of Biological Macromolecules 8 367–371Google Scholar
Gurd, F. R. N. & Wilcox, P. E. 1956 Complex formation between metallic cations and proteins, peptides, and amino acids. Advances in Protein Chemistry 11 311–427Google Scholar
Hayakawa, S. & Nakai, S. 1985 Relationships of hydrophobicity and net charge to the solubility of milk and soy proteins. Journal of Food Science 50 486–491Google Scholar
Heertje, I., Visser, J. & Smits, P. 1985 Structure formation in acid milk gels. Food Microstructure 4 267–277Google Scholar
Hill, R. D. 1970 The effect of the modification of arginine side chains in casein on the coagulation of renninaltered casein. Journal of Dairy Research 37 187–192Google Scholar
Hill, R. D. & Chaker, B. A. 1968 The role of lysine residues in the coagulation of casein. Journal of Dairy Research 35 13–18Google Scholar
Holt, C. 1975 The stability of bovine casein micelles. In Proceedings of the International Conference on Colloid and Surface Science pp. 641–644 (Ed. Wolfram, E.). New York: American Elsevier Publishing Co. Inc.Google Scholar
Holt, C. & Dalgleish, D. G. 1986 Electrophoretic and hydrodynamic properties of bovine casein micelles interpreted in terms of particles with an outer hairy layer. Journal of Colloid and Interface Science 114 513–524Google Scholar
Holt, C., Davies, D. T. & Law, A. J. R. 1986 Effects of colloidal calcium phosphate content and free calcium ion concentration in the milk serum on the dissociation of bovine casein micelles. Journal of Dairy Research 53 557–572Google Scholar
Horne, D. S. 1984 Steric effects in the coagulation of casein micelles by ethanol. Biopolymers 23 989–993Google Scholar
Horne, D. S. & Dalgleish, D. G. 1980 Electrostatic interaction and the kinetics of protein aggregation: αsl-casein. International Journal of Biological Macromolecules 2 154–160Google Scholar
Horne, D. S. & Davidson, C. M. 1986 The effect of environmental conditions on the steric stabilization of casein micelles. Colloid and Polymer Science 264 727–734Google Scholar
Israelachvili, J. N. 1985 a Intermolecular and Surface Forces. New York: Academic PressGoogle Scholar
Israelachvili, J. N. 1985 b Measurements of hydration forces between macroscopic surfaces. Chemica Scripta 25, 7–14Google Scholar
Israelachvili, J. N. & Pashley, R. M. 1982 Double-layer, van der Waals and hydration forces between surfaces in electrolyte solutions. In Biophysics of Water p. 183 (Eds Franks, F. and Mathias, S. F.). New York: John Wiley and SonsGoogle Scholar
Jollès, P., Loucheux-Lefebvre, M. H. & Henschen, A. 1978 Structural relatedness of κ-casein and fibrinogen γ-chain. Journal of Molecular Evolution 11 271–277Google Scholar
Kaye, N. M. C. & Jollés, P. 1978 The involvement of one of the three histidine residues of cow κ-casein in the chymosin-initiated milk clotting process. Biochimica et Biophysica Acta 536 329–340Google Scholar
Lehninger, A. L. 1975 Biochemistry, 2nd edn p. 161. New York: Worth Publishers Inc.Google Scholar
Little, L. 1967 Techniques for acidified dairy products. Journal of Dairy Science 50 434–440Google Scholar
Lumry, R. & Gregory, R. B. 1986 Free-energy management in protein reactions: concepts, complications, and compensation. In The Fluctuating Enzyme pp. 1–189 (Ed. Welch, G. R.). New York: WileyGoogle Scholar
Lumry, R. & Rajender, S. 1970 Enthalpy-entropy compensation phenomena in water solutions of proteins and small molecules: a ubiquitous property of water. Biopolymers 9 1125–1227Google Scholar
Overbeek, J. Th. G. 1982 Colloids, a fascinating subject: introductory lecture. In Colloidal Dispersions pp. 1–21 (Ed. Goodwin, J. W.). London: Royal Society of ChemistryGoogle Scholar
Parker, T. G. & Dalgleish, D. G. 1981 Binding of calcium ions to bovine β-casein. Journal of Dairy Research 48 71–76Google Scholar
Parsegian, V. A. 1982 Physical forces due to the state of water bounding biological materials: some lessons for the design of colloidal systems. Advances in Colloid and Surface Science 16 49Google Scholar
Parsegian, V. A., Fuller, N. & Rand, R. P. 1979 Measured work of deformation and repulsion of lecithin bilayers. Proceedings of the National Academy of Sciences, USA 76 2750–2754Google Scholar
Pashley, R. M. 1985 The effects of hydrated cation adsorption on surface forces between mica crystals and its relevance to colloidal systems. Chemica Scripta 25 22Google Scholar
Pashley, R. M. & Quirk, J. P. 1989 Ion exchange and interparticle forces between clay surfaces. Soil Science Society of America Journal 53 1660Google Scholar
Payens, T. A. J. & Both, P. 1980 Enzymatic clotting processes. IV. The chymosin-triggered clotting of para- κ-casein. In Bioelectrochemistry: ions, surfaces, membranes pp. 130–141 (Ed. Blank, M.). Washington, DC: American Chemical Society (Advances in Chemistry Series No. 188)Google Scholar
Payens, T. A. J. & Vreeman, H. J. 1982 Casein micelles and micelles of κ- and β-casein. In Solution Behavior of Surfactants: theoretical and applied aspects vol. 1 pp. 543–571 (Eds Mittal, K. L. and Fendler, E. J.). New York: Plenum PressGoogle Scholar
Payens, T. A. J., Wiersma, A. K. & Brinkhuis, J. 1977 On enzymatic clotting processes. I. Kinetics of enzyme-triggered coagulation reactions. Biophysical Chemistry 6 253–262Google Scholar
Puri, B. R. & Parkash, S. 1962 Coagulation and electrophoretic behaviour of protein dispersion in milk on the addition of electrolytes. Journal of the Indian Chemical Society 39 605–611Google Scholar
Raap, J., Kerling, K. E. T., Vreeman, H. J. & Visser, S. 1983 Peptide substrates for chymosin (rennin): conformational studies of κ-casein and some κ-casein-related oligopeptides by circular dichroism and secondary structure prediction. Archives of Biochemistry and Biophysics 221 117–124Google Scholar
Roefs, S. P. F. M. 1986 Structure of acid casein gels. PhD Dissertation, Agricultural University, Wageningen, The NetherlandsGoogle Scholar
Sawyer, W. & Hayes, J. F. 1961 A method for the estimation of calcium in casein. Australian Journal of Dairy Technology 16 108–110Google Scholar
Scatchard, G. & Black, E. S. 1949 The effect of salts on the isoionic and isoelectric points of proteins. Journal of Physical and Colloid Chemistry 53 88–99Google Scholar
Scatchard, G., Wu, Y. V. & Shen, A. L. 1959 Physical chemistry of protein solutions. X. The binding of small anions by serum albumin. Journal of the American Chemical Society 81 6104–6109Google Scholar
Schmidt, D. G. & Poll, J. K. 1986 Electrokinetic measurements on unheated and heated casein micelle systems. Netherlands Milk and Dairy Journal 40 269–280Google Scholar
Shortle, D., Meeker, A. K. & Freire, E. 1988 Stability mutants of staphylococcal nuclease: large compensating enthalpy-entropy changes for the reversible denaturation reaction. Biochemistry 27 4761–4768Google Scholar
Snoeren, T. H. M., Payens, T. A. J., Jeunink, J. & Both, P. 1975 Electrostatic interaction between κ carrageenan and κ-casein. Milchwissenschaft 30 393–396Google Scholar
Steven, F. S., Griffin, M. M., Brown, B. S. & Hulley, T. P. 1982 Aggregation of fibrinogen molecules by metal ions. International Journal of Biological Macromolecules 4 367–369Google Scholar
Tanford, C. 1961 Physical Chemistry of Macromolecules p. 461. New York: John Wiley & SonsGoogle Scholar
Van Hooydonk, A. C. M., Hagedoorn, H. G. & Boerrigter, I. J. 1986 a pH-induced physico-chemical changes of casein micelles in milk and their effect on renneting. 1. Effect of acidification on physico-chemical properties. Netherlands Milk and Dairy Journal 40, 281–296Google Scholar
Van Hooydonk, A. C. M., Hagedoorn, H. G. & Boerrigter, I. J. 1986 b The effects of various cations on the renneting of milk. Netherlands Milk and Dairy Journal 40, 369–390Google Scholar
Van Olphen, H. 1977 An Introduction to Clay Colloid Chemistry, 2nd edn.New York: John Wiley and SonsGoogle Scholar
Walstra, P. 1979 The voluminosity of bovine casein micelles and some of its implications. Journal of Dairy Research 46 317–323Google Scholar
Walstra, P., Bloomfield, V. A., Wei, G. J. & Jenness, R. 1981 Effect of chymosin action on the hydrodynamic diameter of casein micelles. Biochimica et Biophysica Acta 669 258–259Google Scholar
Walstra, P. & Jenness, R. 1984 Dairy Chemistry and Physics. New York: John Wiley and SonsGoogle Scholar
White, A., Handler, P. & Smith, E. L. 1964 Principles of Biochemistry, 3rd edn p. 128. New York: McGraw-Hill Book Co.Google Scholar
Zittle, C. A., Dellamonica, E. S., Rudd, R. K. & Custer, J. H. 1958 Binding of calcium to casein: influence of pH and calcium and phosphate concentrations. Archives of Biochemistry and Biophysics 76 342–353Google Scholar