Casein gels consist of a fractal
organized network of aggregated
casein particles. The gel texture thereby depends on the structure,
the spatial distribution, and the interaction forces of the network’s
elementary building blocks. The aim of this study was to explore the
technofunctional consequences of a possible specificity of Maillard
reaction-induced cross-linking reactions on casein with respect to
texture and microstructure of acid gels. Therefore, sodium caseinate
glycated with lactose in the dry state (60 °C, a
w 0.5) was compared with casein samples cross-linked with
methylglyoxal, with glutaraldehyde, or via microbial transglutaminase,
respectively, at similar levels of protein cross-linking as confirmed
by size-exclusion chromatography under denaturing conditions. Casein
gels prepared by acidification with glucono-δ-lactone were characterized
concerning pH kinetics during gelation, mechanical texture properties
under large deformation, and water-holding capacity, while viscometric
properties of casein suspensions were obtained prior to gelation.
The gel microstructure was captured by confocal laser scanning microscopy
and evaluated by means of image texture analysis. All protein cross-linking
reactions studied led to an enhanced gel strength which was accompanied
by an increased interconnectivity of the gel network and a decrease
in apparent pore sizes. Gels with more densely packed strands, as
was the case for enzymatically modified casein, exhibited pronounced
mechanical stability. The spontaneous destabilization of the gel network
upon prolonged glycation reactions, which was not obviously displayed
by microstructural features but connected to an increased viscosity
and pronounced pseudoplastic flow of the unacidified suspension, suggests
a limitation of particle rearrangements and the weakening of interparticle
protein–protein interactions by additional structure attributes
formed during the early Maillard reaction (glycoconjugation).