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Effects of pH and temperature on the water-holding capacity of casein curds and whey protein gels

Published online by Cambridge University Press:  01 June 2009

Cheng Tet Teo ,
Peter A. Munro ,
Harjinder Singh  and
Rocky C. Hudson
Cheng Tet Teo
Affiliation:
Department of Food Technology, Massey University, Palmerston North, New Zealand
Peter A. Munro
Affiliation:
Department of Food Technology, Massey University, Palmerston North, New Zealand
Harjinder Singh
Affiliation:
Department of Food Technology, Massey University, Palmerston North, New Zealand
Rocky C. Hudson
Affiliation:
Department of Food Technology, Massey University, Palmerston North, New Zealand
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Summary

The water-holding capacities of mineral acid casein (MAC) curd, rennet casein curd and whey protein concentrate (WPC) gel were determined as a function of pH and temperature by drainage of liquid on a stationary, horizontal screen. As precipitation pH was varied over the range 4·3–5·55, the water-holding capacity of MAC curd ranged from 2·4 to 5·2 g water/g dry casein with minimum water-holding capacity at precipitation pH 5·3. Samples of dried MAC curd over the same range of precipitation pH did not vary significantly in water-holding capacity, and all absorbed ∼2·0 g water/g dry casein. Both rennet casein curd and WPC (170 g total solids/kg) gels increased in water-holding capacity as the pH of the suspending liquid increased in the range 3·5–10, but the changes with pH were much smaller than for MAC curd. For both types of casein curd and for WPC gel, water-holding capacity decreased with increase in temperature in the range 5–90 °C. The results are interpreted largely in terms of changes in electrostatic interactions with pH and changes in hydrophobic interactions with temperature.

Type
Original Articles
Information
Journal of Dairy Research , Volume 63 , Issue 1 , February 1996 , pp. 83 - 95
Copyright
Copyright © Proprietors of Journal of Dairy Research 1996

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References

REFERENCES

Chan, M. Y. Y., Bell, D. J. & Dunnill, P. 1982 The relationship between the zeta potential and the size of soya protein acid precipitate particles. Biotechnology and Bioengineering 24 1897–1900Google Scholar
Creamer, L. K. 1972 Hydrogen ion equilibria of bovine β-casein-B. Biochimica et Biopkysica Acta 271 252–261CrossRefGoogle Scholar
Diamante, L. M., Munro, P. A. & Weeks, M. G. 1993 Volume, porosity and moisture distribution changes during the drying of rennet, lactic and MAC particles. Transactions of the Institution of Chemical Engineers 71C 33–39Google Scholar
Hobman, P. G. 1978 A model for predicting the water required to wash casein curd. New Zealand Journal of Dairy Science and Technology 13 229–235Google Scholar
Hobman, P. G. & Elston, P. D. 1976 Casein dewheying and dewatering screens. New Zealand Journal of Dairy Science and Technology 11 136–137Google Scholar
Jablonka, M. S. & Munro, P. A. 1985 Particle size distribution and calcium content of batch-precipitated acid casein curd: effect of precipitation temperature and pH. Journal of Dairy Research 52 419–428Google Scholar
Jablonka, M. S. & Munro, P. A. 1986 a Effect of precipitation temperature and pH on the continuous pilot-scale precipitation of acid casein curd. New Zealand Journal of Dairy Science and Technology 21 111–123Google Scholar
Jablonka, M. S. & Munro, P. A. 1986 b Effect of precipitation temperature and pH on the mechanical strength of batch precipitated acid casein curd. Journal of Dairy Research 53 69–73Google Scholar
Kneifel, W., Paquin, P., Abert, T. & Richard, J. -P. 1991 Water-holding capacity of proteins with special regard to milk proteins and methodological aspects – a review. Journal of Dairy Science 74 2027–2041CrossRefGoogle Scholar
Mozhaev, V. V. & Martinek, K. 1984 Structure–stability relationships in proteins: new approaches to stabilizing enzymes. Review. Enzyme and Microbial Technology 6 50–59CrossRefGoogle Scholar
Mulvihill, D. M. 1989 Caseins and caseinates: manufacture. In Developments in Dairy Chemistry—4. Functional Milk Proteins, pp. 97–130 (Ed. Fox, P. F.). London: Elsevier Applied Science.Google Scholar
Munro, P. A. & Stevenson, S. R. 1985 Evaluation of a commercial belt press for the mechanical dewatering of lactic casein curd. New Zealand Journal of Dairy Science and Technology 20 11–18Google Scholar
Munro, P. A. & Tan, B. K. 1984 Inclusion of gas in casein and leaf protein precipitate particles and its effect on particle density. Journal of Chemical Technology and Biotechnology 34B 279–290Google Scholar
Munro, P. A. & Van Til, H. J. 1988 Centrifugal dewatering of acid casein curd: effect of casein manufacturing and centrifugation variables on curd compression in a laboratory centrifuge. Biotechnology and Bioengineering 32 1153–1157CrossRefGoogle Scholar
Munro, P. A. & Vu, J. T. 1983 Optimal operation of a roller press for the mechanical dewatering of acid casein curd: pilot-scale and industrial-scale experiments. New Zealand Journal of Dairy Science and Technology 18 93–100Google Scholar
O'Meara, G. M. & Munro, P. A. 1982 The precipitation and shrinkage of acid casein curd: a preliminary study. New Zealand Journal of Dairy Science and Technology 17 147–159Google Scholar
Pearce, K. N., Johnstone, R. J. & MacColl, A. J. 1987 Computer simulation of continuous multi-stage countercurrent washing of casein curd. New Zealand Journal of Dairy Science and Technology 22 49–66Google Scholar
Roefs, S. P. F. M. 1986 Structure of Acid Casein Gels. A study of gels formed after acidification in the cold. PhD thesis, Wageningen Agricultural University, The Netherlands.Google Scholar
Roefs, S. P. F. M., Van Vliet, T., Van Den Bijgaart, H. J. C. M., De Groot-Mostert, A. E. A. & Walstra, P. 1990 Structure of casein gels made by combined acidification and rennet action. Netherlands Milk and Dairy Journal 44 159–188Google Scholar
Schmidt, D. G. & Poll, J. K. 1986 Electrokinetic measurements on unhealed and heated casein micelle systems. Netherlands Milk and Dairy Journal 40 269–280Google Scholar
Swaisgood, H. E. 1992 Chemistry of the caseins. In Advanced Dairy Chemistry—1. Proteins, pp. 63–110 (Ed. Fox, P. F.). London: Elsevier Applied Science PublishersGoogle Scholar
Teppema, P. & Brouwer, F. 1976 The pH of casein. Netherlands Milk and Dairy Journal 30 79–94Google Scholar
Van Vliet, T. & Walstra, P. 1994 Water in casein gels; how to get it out or keep it in. Journal of Food Engineering 22 75–88CrossRefGoogle Scholar
Virkar, P. D., Hoare, M., Chan, M. Y. Y. & Dunnill, P. 1982 Kinetics of the acid precipitation of soya protein in a continuous flow tubular reactor. Biotechnology and Bioengineering 24 871–887CrossRefGoogle Scholar
Visser, J., Minihan, A., Smits, P., Tjan, S. B. & Heertje, I. 1986 Effects of pH and temperature on the milk salt system. Netherlands Milk and Dairy Journal 40 351–368Google Scholar