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Heat stability of homogenized milk: role of interfacial protein

Published online by Cambridge University Press:  01 June 2009

Catharina H. McCrae ,
David Hirst ,
Andrew J. R. Law  and
D. Donald Muir
Catharina H. McCrae
Affiliation:
Hannah Research Institute, Ayr KA6 5HL, UK
David Hirst
Affiliation:
Hannah Research Institute, Ayr KA6 5HL, UK Scottish Agricultural Statistics Service, Rowett Research Institute, Greenburn Road, Bucksburn, Aberdeen AB2 9SB, UK
Andrew J. R. Law
Affiliation:
Hannah Research Institute, Ayr KA6 5HL, UK
D. Donald Muir
Affiliation:
Hannah Research Institute, Ayr KA6 5HL, UK
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Summary

The role of interfacial protein in determining the heat stability of recombined milk was investigated by removing serum protein prior to homogenization and reincorporating it after homogenization. In addition, the surface protein composition of recombined fat globules was probed by analyses of protein load and by quantification of the individual surface protein components using FPLC. In the absence of serum protein, substantially more casein was bound to the fat surface during homogenization. Despite this, the detrimental effect of homogenization on heat stability did not occur when serum protein had been removed from the system. Reincorporation of serum protein after homogenization caused the heat coagulation time–pH profile to revert to a form very similar to that observed without removing serum protein from the system. Thus, adsorption of serum protein did not affect heat stability. It is more likely that heat-induced interactions of serum protein with surface-adsorbed casein promoted heat coagulation. Fat surface area rather than casein load affected these interfacial protein-protein interactions during heating.

Type
Original articles
Information
Journal of Dairy Research , Volume 61 , Issue 4 , November 1994 , pp. 507 - 516
Copyright
Copyright © Proprietors of Journal of Dairy Research 1994

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References

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