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Relative Emulsifying Activity of Bovine Serum Albumin and Casein as Assessed by Three Different Methods
Author(s) -
HAQUE ZAHURUL,
KINSELLA JOHN E.
Publication year - 1989
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.1365-2621.1989.tb05987.x
Subject(s) - bovine serum albumin , globules of fat , casein , homogenization (climate) , chemistry , homogeneous , chromatography , serum albumin , albumin , food science , biochemistry , biology , milk fat , biodiversity , ecology , physics , thermodynamics , linseed oil
The relative emulsifying activities of bovine serum albumin (BSA) and casein as determined by computerized optical microscopy, electron microscopy and spectroturbidimetry at a protein concentration of 0.135 mM (pH 7) and an oil:water (o:w) ratio of 4:6, was compared. Repeated homogenization led to a more homogeneous distribution of dispersed phase globules. BSA stabilized globules became smaller, e.g. the mean globule diameter determined by the different methods decreased from 3.1 μ at an energy input of 7.6 × 10 7 J m −3 to 2.2μ, at 182 × 10 7 J m −3 . Casein stabilized globules became larger with energy input, e.g. mean d vs increased from 5.0μ at 7.6 × 10 7 J m −3 to 5.8μ. at 182 × 10 7 J m −3 indicating structure dependent differences in the emulsifying activity of protein.