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Thermal gelation of the 12S canola globulin
Author(s) -
Léger Lori W.,
Arntfield Susan D.
Publication year - 1993
Publication title -
journal of the american oil chemists' society
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.512
H-Index - 117
eISSN - 1558-9331
pISSN - 0003-021X
DOI - 10.1007/bf02545343
Subject(s) - guanidine , chemistry , dithiothreitol , differential scanning calorimetry , canola , hydrogen bond , rheology , chemical engineering , hydrochloride , hydrophobic effect , sodium caseinate , thermal stability , zeta potential , chromatography , polymer chemistry , organic chemistry , molecule , materials science , food science , composite material , physics , nanoparticle , engineering , thermodynamics , enzyme
The nature of intermolecular forces responsible for thermal gelation of the 12S canola globulin was determined by preparing gels under a variety of environmental influences. The effects of pH, sodium salts and denaturing agents were evaluated by differential scanning calorimetry, small amplitude oscillatory rheology and transmission light microscopy. Gels prepared with 6% protein at alkaline pH values were superior to gels prepared under acidic conditions. Sodium salts, which promoted protein stability, had an adverse effect on gelation. The addition of guanidine hydrochloride and dithiothreitol to protein dispersions prior to heating produced inferior gels. Hydrophobic forces and electrostatic interactions were responsible for the establishment of canola gel networks. Gel stabilization and strengthening were attributed to disulfide bonding, electrostatic interactions and hydrogen bonding.