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Rennet coagulation of milk in the presence of sucrose

Published online by Cambridge University Press:  01 June 2009

Marie-Hélène Famelart
Marie-Hélène Famelart
Affiliation:
Laboratoire de Recherches de Technologie Laitière, INRA, 65 rue de Saint-Brieuc, 35042 Rennes Cedex, France
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Summary

The aim of this work was to test the diffusion-controlled hypothesis of milk coagulation kinetics by reducing the diffusion coefficient of casein micelles. This has been achieved by increasing the solvent viscosity of milk through sucrose addition. Milk was reconstituted from skim milk powder and sucrose added at 100–300 g kg–1. Hydrolysis and coagulation were followed by chromatographic determination of caseinomacropeptide content and optical, thermal and viscoelastic measurements. Soluble and ionic calcium were determined by atomic absorption spectrophotometry and ionometry and micelle size was measured by dynamic light scattering. Addition of sucrose resulted in a substantial retardation of both enzymic and aggregation steps, a re-equilibration of calcium because of water reduction, and a micelle size increase. The enzymic rate constant was inversely proportional to the viscosity, according to a diffusion-controlled model, and the lag or characteristic times for the aggregation reaction were inversely proportional to the viscosity. These results are consistent with the involvement of diffusion-controlled steps in the sequence of reactions.

Type
Original articles
Information
Journal of Dairy Research , Volume 61 , Issue 4 , November 1994 , pp. 473 - 483
Copyright
Copyright © Proprietors of Journal of Dairy Research 1994

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References

REFERENCES

Bellon, J. L., Quiblier, J. P., Durier, C. & Noel, Y. 1988 [The coagulometer: a new industrial instrument for measurement of milk coagulation time.] Technique Laitière et Marketing no. 1031 29–32Google Scholar
Berridge, N. J. 1952 An improved method of observing the clotting of milk containing rennin. Journal of Dairy Research 19 328–329CrossRefGoogle Scholar
Carlson, A., Hill, C. G. & Olson, N. F. 1987 Kinetics of milk coagulation. II. Kinetics of the secondary phase: micelle flocculation. Biotechnology and Bioengineering 29 590–600CrossRefGoogle ScholarPubMed
Chaplin, B. & Green, M. L. 1980 Determination of the proportion of κ-casein hydrolysed by rennet on coagulation of skim-milk. Journal of Dairy Research 47 351–358CrossRefGoogle Scholar
Chaplin, B. & Green, M. L. 1982 Probing the location of casein fractions in the casein micelle using enzymes and enzyme-dextran conjugates. Journal of Dairy Research 49 631–643CrossRefGoogle Scholar
Darling, D. F. & Dickson, J. 1979 The determination of the zeta potential of casein micelles. Journal of Dairy Research 46 329–332CrossRefGoogle Scholar
Dewan, R. K., Bloomfield, V. A., Chudgar, A. & Morr, C. V. 1973 Viscosity and voluminosity of bovine milk casein micelles. Journal of Dairy Science 56 699–705CrossRefGoogle ScholarPubMed
Ferron-Baumy, C., Molle, D., Garric, G. & Maubois, J. L. 1992 Characterization of caseinomacropeptides released from renneted raw and UHT treated milk. Lait 72 165–173CrossRefGoogle Scholar
Garrett, J. M., Stairs, B. A. & Annett, R. G. 1988 Thermal denaturation and coagulation of whey proteins: effect of sugars. Journal of Dairy Science 71 10–16CrossRefGoogle ScholarPubMed
Geerts, J. P., Bekhof, J. J. & Scherjon, J. W. 1983 Determination of calcium ion activities in milk with an ion-selective electrode. A linear relationship between the logarithm of time and the recovery of the calcium ion activity after heat treatment. Netherlands Milk and Dairy Journal 37 197–211Google Scholar
Green, M. L. & Crutchfield, G. 1971 Density-gradient electrophoresis of native and of rennet-treated casein micelles. Journal of Dairy Research 38 151–164CrossRefGoogle Scholar
Horne, D. S. & Parker, T. G. 1981 Factors affecting the ethanol stability of bovine casein micelles. 3. Substitution of ethanol by other organic solvents. International Journal of Biological Macromolecules 3 399–402CrossRefGoogle Scholar
Korolczuk, J., Maubois, J. L., Cardenas, R. & Grosclaude, G. 1986 Computerized rheometric method for studying rennet coagulation of milk. Lait 66 99–115CrossRefGoogle Scholar
Léonil, J. & Mollé., D. 1991 A method for determination of macropeptide by cation-exchange fast protein liquid chromatography and its use for following the action of chymosin in milk. Journal of Dairy Research 58 321–328CrossRefGoogle Scholar
Lin, S. H. C., Dewan, R. K., Bloomfield, V. A. & Morr, C. V. 1971 Inelastic light-scattering study of the size distribution of bovine milk casein micelles. Biochemistry 10 4788–4793CrossRefGoogle ScholarPubMed
Lin, S. H. C., Leong, S. L., Dewan, R. K., Bloomfield, V. A. & Morr, C. V. 1972 Effect of calcium ion on the structure of native bovine casein micelle. Biochemistry 11 1818–1821CrossRefGoogle Scholar
Marshall, R. J. & Green, M. L. 1980 The effect of the chemical structure of additives on the coagulation of casein micelle suspensions by rennet. Journal of Dairy Research 47 359–369CrossRefGoogle Scholar
Maurel, P. 1978 Relevance of dielectric constant and solvent hydrophobicity to the organic solvent effect in enzymology. Journal of Biological Chemistry 253 1677–1683CrossRefGoogle Scholar
Mozersky, S. M., Farrell, H. M. & Barford, R. A. 1991 The effects of sucrose and lactose on the sizes of casein micelles reconstituted from bovine caseins. Journal of Dairy Science 74 2382–2393CrossRefGoogle Scholar
Muncy, C. A. & Olsen, R. L. 1988 Interaction of protein and polysaccharides in chymosin coagulation of milk. Journal of Dairy Science 71 (Suppl. 1) 65Google Scholar
Olsen, R. L. 1989 Effects of polysaccharides on rennet coagulation of skim milk proteins. Journal of Dairy Science 72 1695–1700CrossRefGoogle Scholar
Payens, T. A. 1984 The relationship between milk concentration and rennet coagulation time. Journal of Applied Biochemistry 6 232–239Google Scholar
Payens, T. A. 1989 The enzyme-triggered coagulation of casein micelles. Advances in Colloid and Interface Science 30 31–69CrossRefGoogle Scholar
Pearce, K. N. 1976 Moving boundary electrophoresis of native and rennet-treated casein micelles. Journal of Dairy Research 43 27–36CrossRefGoogle Scholar
Schmidt, D. G., Both, P. & Koops, J. 1979 Properties of artificial casein micelles. 3. Relationship between salt composition, size and stability towards ethanol, dialysis and heat. Netherlands Milk and Dairy Journal 33 40–48Google Scholar
Tang, Q., Munro, P. A. & McCarthy, O. J. 1993 Rheology of whey protein concentrate solutions as a function of concentration, temperature, pH and salt concentration. Journal of Dairy Research 60 349–361CrossRefGoogle Scholar
Timasheff, S. N. & Arakawa, T. 1989 Stabilization of protein structure by solvents. In Protein Structure: A Practical Approach, pp. 331–345 (Ed. Creighton, T. E.). Oxford: IRL PressGoogle Scholar
Tomassone, R., Lesquoy, E. & Millier, C. 1983 [Regression. A new approach using an old statistical technique,] pp. 160–162Paris: Masson (INRA Actualités Scientifiques et Agronomiques)Google Scholar
Van Hooydonk, A. C. M., Olieman, C. & Hagedoorn, H. G. 1984 Kinetics of the chymosin-catalysed proteolysis of κ-casein in milk. Netherlands Milk and Dairy Journal 38 207–222Google Scholar
Van Hooydonk, A. C. M. & Van Den Berg, G. 1988 Control and determination of the curd-setting during cheesemaking. International Dairy Federation Bulletin no. 225 2–10Google Scholar
Van Hooydonk, A. C. M. & Walstra, P. 1987 Interpretation of the kinetics of the renneting reaction in milk. Netherlands Milk and Dairy Journal 41 19–47Google Scholar