RESUMO
The dynamics of rigid dendrimer and flexible PEG probes in sodium caseinate dispersions and acid gels, including both translational diffusion and rotational diffusion, were studied by NMR. Above the onset of the close-packing limit (C â¼ 10 g/100 g H2 O), translational diffusion of the probe depended on its flexibility and on the fluctuations of the matrix chains. The PEG probe diffused more rapidly than the spherical dendrimer probe of corresponding hydrodynamic radius. The greater conformational flexibility of PEG facilitated its motion through the crowded casein matrix. Rotational diffusion was, however, substantially less hindered than the translational diffusion and depended on the local protein-probe friction which became high when the casein concentration increased. The coagulation of the matrix led to the formation of large voids, which resulted in an increase in the translational diffusion of the probes, whereas the rotational diffusion of the probes was retarded in the gel, which could be attributed to the immobilized environment surrounding the probe. Quantitative information from PFG-NMR and SEM micrographs have been combined for characterizing microstructural details in SC acid gels.
Assuntos
Ácidos/química , Caseínas/química , Dendrímeros/química , Géis/química , Polietilenoglicóis/química , Difusão , Microscopia Eletrônica de Varredura , Porosidade , Rotação , Fatores de TempoRESUMO
Pulsed field gradient nuclear magnetic resonance and proton nuclear magnetic resonance relaxometry were used to study the self-diffusion coefficients and molecular dynamics of linear (PEGs) and spherical probes (dendrimers) in native phosphocaseinate suspensions and in a concentrated rennet gel. It was shown that both the size and the shape of the diffusing molecules and the matrix topography affected the diffusion and relaxation rates. In suspensions, both translational and rotational diffusion decreased with increasing casein concentrations due to increased restriction in the freedom of motion. Rotational diffusion was, however, less hindered than translational diffusion. After coagulation, translational diffusion increased but rotational diffusion decreased. Analysis of the T2 relaxation times obtained for probes of different sizes distinguished the free short-chain relaxation formed from a few monomeric units from (i) the relaxation of protons attached to long polymer chains and (ii) the short-chain relaxation attached to a rigid dendrimer core.