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-linked hydrogel. The larger-molecular-weight proteins have lower diffusivity (D(e)) in the hydrogel. Increasing temperature accelerated the diffusion rate of proteins; however, the diffusion did not follow the Arrhenius equation at temperatures above 37 °C. The swelling ratio of the hydrogel was slightly decreased 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 over 37 °C. The model proteins have high affinities to buffer solution compared to the hydrogel network structure, resulting in high partition coefficients (K > 1) which do not affect the calculation of D(e) values. Incorporated protein release follows the theory of hindered diffusion.
Original language | English (US) |
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Pages (from-to) | 5658-5665 |
Number of pages | 8 |
Journal | Journal of Agricultural and Food Chemistry |
Volume | 48 |
Issue number | 11 |
DOIs | |
State | Published - 2000 |
Keywords
- Hindered diffusion
- Hydrogel
- Partition coefficient
- Protein delivery systems
- Swelling ratio
- Viscosity
ASJC Scopus subject areas
- Agricultural and Biological Sciences (miscellaneous)
- Food Science
- Chemistry (miscellaneous)