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Emulsifying Properties of Food Proteins: Bovine Serum Albumin
Author(s) -
HAQUE Z.AHURUL,
KINSELLA J.OHN E.
Publication year - 1988
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1365-2621.1988.tb07719.x
Subject(s) - bovine serum albumin , emulsion , chemistry , chromatography , viscosity , serum albumin , albumin , biochemistry , materials science , composite material
Emulsifying activity (EA) of bovine serum albumin (BSA), at concentrations of 0.07 to 0.45 mM, was maximum at oil:water ratios (o:w) <2:8, in the pH range 4 to 8. At pH 8, the EA was greater than that at pH values below, i.e., < pH 7, but the energy required to form emulsions was higher., EA and emulsion stability (ES) were directly related and improved in NaCl; ES was maximum at pH 4. Surface load was directly related to the o:w and the increase in viscosity with protein load apparently reflected protein unfolding that was marked at an energy input of 680 10 6 J m ‐3 . Data indicate that some native structure and flexibility of the BSA molecule are required for optimum emulsifying properties.