| Abstract
| - Lactitol-based cross-linked hydrogel was synthesized, and model proteins (α-chymotrypsin, β-lactoglobulin, bovine serum albumin (BSA), and γ-globulin) were incorporated into the cross-linkedhydrogel. The larger-molecular-weight proteins have lower diffusivity (De) in the hydrogel. Increasingtemperature accelerated the diffusion rate of proteins; however, the diffusion did not follow theArrhenius equation at temperatures above 37 °C. The swelling ratio of the hydrogel was slightlydecreased after heating for 2 h at 37 and 45 °C, and significantly reduced after 1 h at 60 °C. Therefore,diffusion of β-lactoglobulin and BSA may be decreased by hydrogel shrinking at temperature over37 °C. The model proteins have high affinities to buffer solution compared to the hydrogel networkstructure, resulting in high partition coefficients (K> 1) which do not affect the calculation of Devalues. Incorporated protein release follows the theory of hindered diffusion. Keywords: Protein delivery systems; hindered diffusion; hydrogel; viscosity; swelling ratio; partitioncoefficient
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