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Haque, Z.U. and Kinsella, J.E. (1989) Relative Emulsifying Activity of Bovine Serum Albumin and Casein as Assessed by Three Different Methods. Journal of Food Science, 54, 1341-1344.
http://dx.doi.org/10.1111/j.1365-2621.1989.tb05987.x

has been cited by the following article:

• TITLE: Influence of Small Amphiphiles on Aqueous Dispersions of β-Lactoglobulin A and Bovine Serum Albumin: (2) Surface Energy and Emulsifying Properties

  AUTHORS: Zahur Z. Haque, Guichard L. Bohoua

  KEYWORDS: Functionality, Emulsion, Surface Energy, Interface, Stability, Surfactant

  JOURNAL NAME: Food and Nutrition Sciences, Vol.6 No.12, September 24, 2015

  ABSTRACT: Influence of amphiphiles on surface energy (γ), emulsifying activity index (EAI) and emulsion stability (ES) of fatty-acid free bovine serum albumin (FAF-BSA), bovine serum albumin (BSA), and β-lactoglobulin A (β-LGA) was studied. Contact angle measurements (θ) of sessile drops of protein-surfactant mixtures were determined using water and α-bromonaphthalene as solvents of known parameters to calculate γ. All surfactants except zwitterionic Z8 increased γ. The greatest increase was by anionic SDS. All surfactants significantly reduced EAI in spite of increased γ. ES was reduced by all surfactants except cationic TDTM which, conversely, enhanced ES by up to 186% for BSA and β-LGA.