Melting of the Ovalbumin Gels by Heating: Reversibility between Gel and Sol

Abstract

Heat-induced ovalbumin gels prepared under given conditions were melted with a second heating to below 90°C. The sample melted was gelled again on cooling. This gel-sol transition, which was detected both by eye and by the change in the dynamic viscoelastic parameters G' and G", was reversible. Differential scanning calorimetry showed that the endothermic heat flow that accompanied the gel-sol transition was much lower than that accompanied the denaturation of ovalbumin. With the repetition of the gel-sol transition, intermolecular disulfide bridges were formed, detected by sodium dodecyl sulfate-polyacrylamide electrophoresis done without a reducing agent.