Article ID Journal Published Year Pages File Type
1988158 International Journal of Biological Macromolecules 2006 5 Pages PDF
Abstract

The physical properties and microstructure of gelatin–maltodextrin hydrogels fixed with genipin (GP) were investigated as a function of pH (3–7), maltodextrin (MD) (0–9%, w/w) and GP (0–10 mM levels), at a constant gelatin (G) concentration (10%, w/w). Network strength (elastic modulus, E) and swelling behavior were characterized by large deformation testing and by swelling index (SI). In general, network strength increased and swelling decreased at higher pH, MD and GP levels, except at pH 3, where E was independent of the GP concentration until ∼7.5 mM, above which it declined. Confocal scanning laser microscopy (CLSM) images showed phase separation to be suppressed at pH 3, whereas at pH 7, separation into a self-similar dispersed phase was apparent. Overall, the judicious use of GP to crosslink G was an appropriate means of kinetically trapping MD within the gelatin network.

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