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We investigated mixed-protein gels made from sodium caseinate and ovalbuminat different ratios with use of the acidification agentglucono-$\delta$-lactone. Dynamic viscoelastic measurements revealed thatincreasing the ovalbumin content decreased the mechanical properties of the gelbut accelerated onset time of the phase transition. Ultrasound spectroscopyduring gelation revealed that the relative velocity gradually decreased,whereas the ultrasonic attenuation increased during the whole acidificationprocess until gelation was complete, although these changes were much smallerthan those observed with heat-induced gelation. Confocal laser scanningmicroscopy along with scanning electron microscopy revealed that althoughuniform mixing of sodium caseinate and ovalbumin was observed, sodium caseinateis likely to mainly lead formation of the gel network, and the porosity of theresulting gel network depends on the ratio of these two components. The resultsdemonstrate that confocal laser scanning microscopy is a useful tool foranalyzing both the networks within mixed-protein gels and the contribution ofeach protein to the network and gelation.

colloids and surfaces b biointerfaces

Characterization of the gelation and resulting network of a  mixed-protein gel derived from sodium caseinate and ovalbumin in the presence  of glucono-$\delta$-lactone