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A Comparison Between Ovalbumin Gels Formed by Heat and by Guanidinium Hydrochloride Denaturation
Author(s) -
EGELANDSDAL B.
Publication year - 1984
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.1365-2621.1984.tb10402.x
Subject(s) - denaturation (fissile materials) , chemistry , ovalbumin , hydrochloride , guanidine , chromatography , guanidinium chloride , solubility , nuclear chemistry , organic chemistry , enzyme , immune system , immunology , biology
Ovalbumin was denatured by heat or by addition of 6M guanidinium hydrochloride (GuHCl) at pH 2.5. Denaturation by heat led to immediate gel formation whereas denaturation by GuHCl yielded gels only after subsequent removal of the denaturant. The two types of gels formed were compared by using texture measurements. Chemically denatured molecules had the largest hydrodynamic volume and also formed the hardest gels (protein concentration: 6% w/v). This difference in gel hardness was, however, much enhanced if the denaturant was slowly removed from the protein solution. Hence, the rate of gel formation appears to be of greater consequence than the degree of protein unfolding for the hardness of the gels formed.