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Surface Properties and Emulsification Behavior of Denatured Soy Proteins
Author(s) -
NIR I.,
FELDMAN Y.,
ASERIN A.,
GARTI N.
Publication year - 1994
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.1365-2621.1994.tb05573.x
Subject(s) - guanidine , soy protein , chemistry , urea , chromatography , cleavage (geology) , fluorescence , organic chemistry , biochemistry , materials science , fracture (geology) , composite material , physics , quantum mechanics
Soy protein isolate was physically (heat pretreatment) and chemically (urea, guanidine·HCl, and cleavage of SS bonds) modified in order to dissociate subunits, unfold the protein and improve surface properties: hydrophobicity, emulsification capability, and stability. Heat pretreatment as well as chemical treatment with urea or guanidine·HCl or reduction of disulphide bonds, will improve emulsification performance in comparison to native soy protein isolate. Significant differences in reduction of surface tension of water in the presence of native and modified proteins were observed (45 and 35 dynes/cm respectively). Measurements of fluorescence indicated that the relative hydrophobicity of the soy protein was also improved (from 600 to 1360) after heat pretreatment or contacting the soy protein with 8M urea solution.