Free Access
Dairy Sci. Technol.
Volume 90, Number 2-3, March–June 2010
Special Issue: Selected papers from 4th International Symposium on Spray Dried Dairy Products,
15-17th April 2009, Melbourne, Australia
Page(s) 169 - 179
Published online 19 January 2010
  1. Allison S.D., Chang B., Randolph T.W., Carpenter J.F., Hydrogen bonding between sugar and protein is responsible for inhibition of dehydration-induced protein unfolding, Arch. Biochem. Biophys. 365 (1999) 289–298. [CrossRef] [PubMed] [Google Scholar]
  2. Allison S.D., Dong A., Carpenter J.F., Counteracting effects of thiocyanate and sucrose on chymotrypsinogen secondary structure and aggregation during freezing, drying, and rehydration, Biophys. J. 71 (1996) 2022–2032. [CrossRef] [PubMed] [Google Scholar]
  3. American Dry Milk Institute, Determination of solubility index, in: Bulletin 916 (Revised), Standards for Grades of Dry Milks Including Methods of Analysis, American Dry Milk Institute Inc., Chicago, Illinois, USA, 1971, pp. 26–27. [Google Scholar]
  4. Aneja R.P., Equipment for recombination, in: Recombination of Milk and Milk Products, Alexandria, Egypt, 12–16 November 1988, Special Issue 9001, Int. Dairy Fed., Brussels, Belgium, 1988, pp. 186–195. [Google Scholar]
  5. Anema S.G., Li Y., Re-equilibration of the minerals in skim milk during reconstitution, Milchwissenschaft 58 (2003) 174–178. [Google Scholar]
  6. Anema S.G., Pinder D.N., Hunter R.J., Hemar Y., Effects of storage temperature on the solubility of milk protein concentrate (MPC85), Food Hydrocoll. 20 (2006) 386–393. [CrossRef] [Google Scholar]
  7. Aoki T., Umeda T., Nakano T., Effect of sodium chloride on the properties of casein micelles, Milchwissenschaft 54 (1999) 91–93. [Google Scholar]
  8. Baldwin A., Pearce D., Milk powder, in: Onwulata C. (Ed.), Encapsulated and Powdered Foods, Taylor & Francis, Boca Raton, Florida, USA, 2005, pp. 387–433. [CrossRef] [Google Scholar]
  9. Baldwin A.J., Truong G.N.T., Development of insolubility in dehydration of dairy milk powders, Food Bioprod. Process. 85 (C3) (2007) 202–208. [CrossRef] [Google Scholar]
  10. Cho Y., Singh H., Creamer L.K., Heat-induced interactions of β-lactoglobulin A and κ-casein B in a model system, J. Dairy Res. 70 (2003) 61–71. [CrossRef] [MathSciNet] [PubMed] [Google Scholar]
  11. Creighton T.E., Proteins: Structures and Molecular Principles, W.H. Freeman and Co., New York, USA, 1984, pp. 139–152. [Google Scholar]
  12. de Kruif C.G., Holt C., Casein micelle structure, functions and interactions, in: Fox P.F., McSweeney P.L.H. (Eds.), Advanced Dairy Chemistry. 1. Proteins, Part A, 3rd edn., Kluwer Academic/Plenum Publishers, New York, USA, 2003, pp. 233–276. [Google Scholar]
  13. Edsall J.T., McKenzie H.A., Water and proteins. II. The location and dynamics of water in protein systems and its relation to their stability and properties, Adv. Biophys. 16 (1983) 53–183. [CrossRef] [PubMed] [Google Scholar]
  14. Eino M., The manufacture of recombined condensed milk, in: Recombination of Milk and Milk Products, Alexandria, Egypt, 12–16 November 1988, Special Issue 9001, Int. Dairy Fed., Brussels, Belgium, 1990, pp. 351–363. [Google Scholar]
  15. Ellis J.R., Prillig E.B., Amann A.H., Tablet coating, in: Lachman L., Lieberman H.A., Karig J.L. (Eds.), The Theory and Practice of Industrial Pharmacy, 2nd edn., Lea & Febiger, Philadelphia, Pennsylvania, USA, 1976, pp. 359–388. [Google Scholar]
  16. Fox P.F., Brodkorb A., The casein micelle: historical aspects, current concepts and significance, Int. Dairy J. 18 (2008) 677–684. [CrossRef] [Google Scholar]
  17. Gaiani C., Schuck P., Scher J., Desobry S., Banon S., Dairy powder rehydration: influence of protein state, incorporation mode, and agglomeration, J. Dairy Sci. 90 (2007) 570–581. [CrossRef] [PubMed] [Google Scholar]
  18. Gaucheron F., Le Graet Y., Briard V., Effect of NaCl addition on the mineral equilibrium of concentrated and acidified casein micelles, Milchwissenschaft 55 (2000) 82–86. [Google Scholar]
  19. Gregory R.B., Protein hydration and glass transitions, in: Reid D.S. (Ed.), The Properties of Water in Foods ISOPOW 6, Blackie Academic & Professional, London, UK, 1998, pp. 57–99. [Google Scholar]
  20. Griffin M.C.A., Lyster R.L.J., Price J.C., The disaggregation of calcium-depleted casein micelles, Eur. J. Biochem. 174 (1988) 339–343. [CrossRef] [PubMed] [Google Scholar]
  21. Grufferty M.B., Fox P.F., Effect of added NaCl on some physicochemical properties of milk, Ir. J. Food Sci. Technol. 9 (1985) 1–9. [Google Scholar]
  22. Hall C.W., Hedrick T.I., Drying of Milk and Milk Products, 2nd edn., AVI Publishing Co. Inc., Westport, Connecticut, USA, 1971, pp. 103–105, 215–216. [Google Scholar]
  23. Harland H.A., Coulter S.T., Jenness R., The effect of the various steps in the manufacture on the extent of serum protein denaturation in nonfat dry milk solids, J. Dairy Sci. 35 (1952) 363–368. [CrossRef] [Google Scholar]
  24. Havea P., Protein interactions in milk protein concentrate powders, Int. Dairy J. 16 (2006) 415–422. [CrossRef] [Google Scholar]
  25. Horne D.S., Casein interactions: casting light on the black boxes, the structure in dairy products, Int. Dairy J. 8 (1998) 171–177. [CrossRef] [Google Scholar]
  26. Huppertz T., Fox P.F., Effect of NaCl on some physico-chemical properties of concentrated bovine milk, Int. Dairy J. 16 (2006) 1142–1148. [CrossRef] [Google Scholar]
  27. International Dairy Federation, Dried milk and dried milk products – determination of insolubility index, IDF Standard 129, Int. Dairy Fed., Brussels, Belgium, 2005. [Google Scholar]
  28. Jeantet R., Schuck P., Six T., Andre C., Delaplace G., The influence of stirring speed, temperature and solid concentration on the rehydration time of micellar casein powder, Dairy Sci. Technol., DOI: 10.1051/dst/2009043. [Google Scholar]
  29. Kudo N., Hols G., van Mil P.J.J.M., The insolubility index of moist skim milk powder: influence of the temperature of the secondary drying air, Neth. Milk Dairy J. 44 (1990) 89–98. [Google Scholar]
  30. Kunz I.D., The physical properties of water associated with biomacromolecules, in: Duckworth R.B. (Ed.), Water Relations of Foods, Academic Press, London, UK, 1974, pp. 93–109. [Google Scholar]
  31. Lampitt L.H., Bushill J.H., The physico-chemical constitution of milk powder, Analyst 56 (1931) 778–794. [CrossRef] [Google Scholar]
  32. Martin G.J.O., Williams R.P.W., Dunstan D.E., Comparison of casein micelles in raw and reconstituted skim milk, J. Dairy Sci. 90 (2007) 4543–4551. [CrossRef] [PubMed] [Google Scholar]
  33. McKenna A.B., Effects of processing and storage on the reconstitution properties of whole milk and ultrafiltered skim milk powders, Ph.D. Thesis, Massey University, Palmerston North, New Zealand, 2000. [Google Scholar]
  34. New Zealand Dairy Board, Milk protein products and process, Patent WO 01/41578, 2001. [Google Scholar]
  35. New Zealand Dairy Board, Monovalent salt enhances solubility of milk protein concentrate, Patent WO 02/096208, 2002. [Google Scholar]
  36. Nielsen L.S., Fee C.J., Chen X.D., The effects of temperature and holding time of external heating on solubility deterioration of a skim milk powder, Trans. IChemE 74 (Part C) (1996) 159–162. [Google Scholar]
  37. Patel H.A., Singh H., Anema S.G., Creamer L.K., Effects of heat and high hydrostatic pressure treatments on disulfide bonding interchanges among the proteins in skim milk, J. Agric. Food Chem. 54 (2006) 3409–3420. [CrossRef] [PubMed] [Google Scholar]
  38. Pisecky J., Handbook of Milk Powder Manufacture, Niro A/S, Copenhagen, Denmark, 1997, pp. 151–153. [Google Scholar]
  39. Prestrelski S.J., Tedeschi N., Arakawa T., Carpenter J.F., Dehydration-induced conformational transitions in proteins and their inhibition by stabilizers, Biophys. J. 65 (1993) 661–671. [CrossRef] [PubMed] [Google Scholar]
  40. Qi P.X., Studies of casein micelle structure: the past and the present, Lait 87 (2007) 363–383. [CrossRef] [EDP Sciences] [Google Scholar]
  41. Rahman M.S., Glass transition data and models of foods, in: Rahman M.S. (Ed.), Food Properties Handbook, 2nd edn., CRC Press, Boca Raton, Florida, USA, 2009, p. 268. [Google Scholar]
  42. Schuck P., Davenel A., Mariette F., Briard V., Méjean S., Piot M., Rehydration of casein powders: effects of added mineral salts and salt addition methods on water transfer, Int. Dairy J. 12 (2002) 51–57. [CrossRef] [Google Scholar]
  43. Schuck P., Piot M., Méjean S., Le Graët Y., Fauquant J., Brulé G., Maubois J.-L., Déshydratation par atomisation de phosphocaséinate natif obtenu par microfiltration sur membrane, Lait 74 (1994) 375–388. [CrossRef] [EDP Sciences] [Google Scholar]
  44. van Hooydonk A.C.M., Hagedoorn H.G., Boerrigter I.J., The effect of various cations on the renneting of milk, Neth. Milk Dairy J. 40 (1986) 369–390. [Google Scholar]
  45. Walstra P., Casein sub-micelles: do they exist?, Int. Dairy J. 9 (1999) 189–192. [CrossRef] [Google Scholar]
  46. Walstra P., Jenness R., Dairy Chemistry and Physics, John Wiley & Sons, New York, USA, 1984, p. 106. [Google Scholar]
  47. Walstra P., Jenness R., Dairy Chemistry and Physics, John Wiley & Sons, New York, USA, 1984, pp. 229–253. [Google Scholar]
  48. Walstra P., Jenness R., Dairy Chemistry and Physics, John Wiley & Sons, New York, USA, 1984, pp. 307–309. [Google Scholar]
  49. Wright N.C., Factors affecting the solubility of milk powders. 1. The effect of heat on the solubility of milk proteins, J. Dairy Res. 4 (1933) 122–141. [CrossRef] [Google Scholar]