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Disulfide Bond Formation Affects Stability of Whey Protein Isolate Emulsions
Author(s) -
McCLEMENTS D.J.,
MONAHAN F.J.,
KINSELLA J.E.
Publication year - 1993
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.1365-2621.1993.tb06106.x
Subject(s) - chemistry , flocculation , chromatography , whey protein , disulfide bond , whey protein isolate , emulsion , hexadecane , chemical engineering , organic chemistry , biochemistry , engineering
The viscosity and degree of flocculation of 20 wt% n‐hexadecane oil‐in‐water emulsions stabilized by whey protein isolate (1 wt% WPI in 0.05M phosphate buffer, pH 7.0) increased as the emulsions aged. These effects were reduced when N‐ethylmaleimide, a sulfhydryl blocking agent, was added to the emulsions immediately after homogenization, but were not completely eliminated. Gel electrophoresis (SDS‐PAGE) showed an increase in the extent of intermolecular disulfide bond formation between proteins absorbed at the droplet interface with time. Floes were probably formed initially by noncovalent bonding or bridging flocculation, and then stabilized by disulfide bonds between proteins absorbed to different droplets.