To better tailor gelatins for textural characteristics in (food) gels, their interactions are destabilized by introduction of electrostatic repulsions and creation of affinity sites for calcium to “lock” intermolecular interactions. For that purpose gelatins with various degrees of succinylation are obtained. Extensive succinylation hampers helix formation and gel strength is slightly reduced. At high degrees of succinylation the helix propensity, gelling/melting temperatures, concomitant transition enthalpy, and gel strength become calcium-sensitive, and relatively low calcium concentrations largely restore these properties. Although succinylation has a major impact on the brittleness of the gels formed and the addition of calcium makes the material less brittle compared to nonmodified gelatin, the modification has no impact on the energy balance in the gel, where all energy applied is elastically stored in the material. This is explained by the unaffected stress relaxation by the network and high water-holding capacity related to the small mesh sizes in the gels.
- protein gel
- Calcium binding
Baigts Allende, D., & de Jongh, H. H. J. (2015). Calcium binding restores gel formation of succinylated gelatin and reduces brittleness with preservation of the elastically stored energy. Journal of Agricultural and Food Chemistry, 63, 7058-7065. https://doi.org/10.1021/acs.jafc.5b01962