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

CLSM image of acidified 5% SC + 5% OVA mixed gel (pH4.2). [Display omitted] •Mixed protein gels were analyzed by staining with different fluorescent dyes.•Sodium caseinate leaded gelation of the mixture with OVA under acidification.•CLSM observation could clarify the contribution of respective proteins in mixed gels. We investigated mixed-protein gels made from sodium caseinate and ovalbumin at different ratios with use of the acidification agent glucono-δ-lactone. Dynamic viscoelastic measurements revealed that increasing the ovalbumin content decreased the mechanical properties of the gel but accelerated onset time of the phase transition. Ultrasound spectroscopy during gelation revealed that the relative velocity gradually decreased, whereas the ultrasonic attenuation increased during the whole acidification process until gelation was complete, although these changes were much smaller than those observed with heat-induced gelation. Confocal laser scanning microscopy along with scanning electron microscopy revealed that although uniform mixing of sodium caseinate and ovalbumin was observed, sodium caseinate is likely to mainly lead formation of the gel network, and the porosity of the resulting gel network depends on the ratio of these two components. The results demonstrate that confocal laser scanning microscopy is a useful tool for analyzing both the networks within mixed-protein gels and the contribution of each protein to the network and gelation.