The network structure of native and carbodiimide cross-linked gelatin A and
B gels was studied based on their rheological behavior. Gelatin A and B co
ntain different numbers of carboxylic acid groups caused by different prepa
ration conditions and had previously shown different characteristics in con
trolled release applications. It was evaluated to which extent chemical cro
ss-linking densified the network structure of physical gelatin gels. After
normalization of the equilibrium shear modulus (G(e)) with respect to swell
ing (Q), it was observed that the normalized G(e) values largely depend on
the way gelatin is prepared from collagen. At an equal number of chemical j
unctions, chemically cross-linked gelatin B gels had a lower elasticity mod
ulus than chemically cross-linked gelatin A gels. This seemed contradictory
as gelatin B contains more carboxylic acid groups, available for cross-lin
king, but is related to a higher probability for intramolecular cross-linki
ng, as was validated quantitatively by chemical and rheological analysis of
the number of cross-links. Assuming an ideal network, the average molecula
r weight of the elastic network chains (M-c) was calculated for physical an
d chemical gelatin A and B networks, and on the basis of M-c the mesh sizes
of the gels were estimated. The calculated mesh sizes were experimentally
confirmed by lysozyme and albumin diffusion. Chemical cross-linking increas
ed the resistance of the gels toward thermal degradation, resulting in a mo
re gradual disintegration of physical cross-links upon heating. Moreover, c
hemical cross-linking prevented recombination of these cross-links upon coo
ling.