No abstract

No abstract

The structural behavior of a well-characterized gelatin sample has been revisited to investigate the morphology of its network in the presence of sugar. This was then contrasted with the corresponding properties of the gelling polysaccharides agarose, kappa-carrageenan, and deacylated gellan. Small deformation dynamic oscillation, differential scanning calorimetry in plain and modulated mode, visual observations, and transmission electron microscopy were used to identify the structural characteristics of the biopolymers from the rubbery plateau through the transition region to the glassy state. In contrast to the collapse of the polysaccharide gels at intermediate levels of co-solute, gelatin forms reinforced networks. The drop in polysaccharide network strength is accompanied by a decline in the enthalpy of the coil-to-helix transition, whereas the transition enthalpy is more pronounced in gelatin gels in accordance with their strengthening. Tangible evidence of the molecular transformations was obtained using microscopy, with polysaccharides disaggregating and dissolving in the saturated sugar environment. Gelatin, on the other hand, is visualized in an aggregated form thus producing a phase-separated topology with sugar.

The physiological importance of weak interactions between biological macromolecules (molar dissociation constants >10 microM) is now well recognized, particularly with regard to cell adhesion and immunological phenomena, and many weak interactions have been measured for proteins. The concomitant importance of carbohydrate-carbohydrate interactions has also been identified, although no weak interaction between pure carbohydrate systems has ever been measured. We now demonstrate for the first time to our knowledge using a powerful probe for weak interactions--sedimentation velocity in the analytical ultracentrifuge--that at least some carbohydrates (from the class of polysaccharides known as heteroxylans and demonstrated here to be biologically active) can show well-defined weak self-interactions of the "monomer-dimer" type frequently found in protein systems. The weak interaction between the heteroxylans is shown from a temperature dependence study to be likely to be hydrophobic in nature.

No abstract