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HEAT‐INDUCED GELLING IN SOLUTIONS OF OVALBUMIN
Author(s) -
EGELANDSDAL BJØRG
Publication year - 1980
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.1365-2621.1980.tb04103.x
Subject(s) - ovalbumin , isoelectric point , ionic strength , chemistry , ionic bonding , pi , chromatography , chemical engineering , thermodynamics , organic chemistry , aqueous solution , biochemistry , ion , physics , enzyme , engineering , biology , immune system , immunology
The heat‐induced gelling of ovalbumin solutions (8.2%) has been studied as a function of pH and ionic strength. At low ionic strengths, plots of gel rigidity against pH passed through a maximum on each side of the isoelectric point (PI). The maximum on the acid side had a higher absolute value and occurred at a higher net charge on the protein than the one on the alkaline side. Increasing the ionic strength shifted the two maxima away from the PI. The results suggest that ovalbumin gelling is governed primarily by electrostatic forces.