Structural characteristics and foaming properties of β-lactoglobulin: Effects of shear rate and temperature

L. G. Phillips, S. E. Hawks, J. B. German

Research output: Contribution to journalArticle

43 Scopus citations

Abstract

The main purpose of this study was to determine the extent to which the process of foaming changes the structure ob β-lactoglobulin (β-Lg). β-Lg unfolded while existing as a foam, but changes in conformation were reversible upon collapse of the foam. A plot of the overrun (a measure of air incorporation in the foam) for β-Lg foams (pH 7) versus temperature (3-45°C) was a sigmoidal curve that resembled a two-state denaturation curve. Foaming properties were influenced by temperature and pH, which was attributed to differences in protein structure, in diffusion rate and in the number of molecules in solution for β-Lg at pH 9 as compared to pH 7. There was a strong correlation (r > 0.9) between the secondary structure of β-Lg in solution and the observed foaming properties. A direct link between the structure of β-Lg in solution and its foaming properties was established.

Original languageEnglish (US)
Pages (from-to)613-619
Number of pages7
JournalJournal of Agricultural and Food Chemistry
Volume43
Issue number3
StatePublished - 1995

Keywords

  • β-Lg functionality
  • β-Lg structure
  • Foam
  • Foaming properties

ASJC Scopus subject areas

  • Agricultural and Biological Sciences (miscellaneous)
  • Food Science
  • Chemistry (miscellaneous)

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