Relationships Between Hydrophobicity and Foaming Characteristics of Food Proteins

Authors

  • ALTHEA-ANN TOWNSEND,

    1. Authors Townsend and Nakai are affiliated with the Dept. of Food Science, Univ. of British Columbia, Vancouver, B.C., Canada V6T 2A2.
    Search for more papers by this author
  • SHURYO NAKAI

    1. Authors Townsend and Nakai are affiliated with the Dept. of Food Science, Univ. of British Columbia, Vancouver, B.C., Canada V6T 2A2.
    Search for more papers by this author

  • This work was performed as part of NSERC project No. A3641 supported by the Natural Sciences & Engineering Research Council of Canada.

ABSTRACT

Hydrophobocity measured fluorometrically for food proteins and pure proteins using cis-parinaric acid as a hydrophobic probe had significant correlations to foaming capacity when the proteins in solution were unfolded by heating in boiling water in the presence of 1.5% dodecyl sulphate prior to fluorometric measurement. Hydrophobicity measured without unfolding, which had previously shown a significant correlation to emulsification, was not significantly correlated with foaming capacity. Two highly significant regression equations were generated: one included hydrophobicity and dispersibility and the other, hydrophobicity and viscosity as the independent variables. High hydrophobicity and viscosity and moderate dispersibility were associated with optimum foaming capacity. There was a significant negative relationship between foam stability and charge density. Hydrophobicity and viscosity were also important in foam stability.

Ancillary