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) |
|---|---|
| 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 |
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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)
Cite this
Mechanism and characteristics of protein release from lactitol-based cross-linked hydrogel. / Han, Jung H.; Krochta, John M.; Hsieh, You Lo; Kurth, Mark J.
In: Journal of Agricultural and Food Chemistry, Vol. 48, No. 11, 2000, p. 5658-5665.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Mechanism and characteristics of protein release from lactitol-based cross-linked hydrogel
AU - Han, Jung H.
AU - Krochta, John M.
AU - Hsieh, You Lo
AU - Kurth, Mark J.
PY - 2000
Y1 - 2000
N2 - 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.
AB - 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.
KW - Hindered diffusion
KW - Hydrogel
KW - Partition coefficient
KW - Protein delivery systems
KW - Swelling ratio
KW - Viscosity
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UR - http://www.scopus.com/inward/citedby.url?scp=0033667606&partnerID=8YFLogxK
U2 - 10.1021/jf0002239
DO - 10.1021/jf0002239
M3 - Article
C2 - 11087535
AN - SCOPUS:0033667606
VL - 48
SP - 5658
EP - 5665
JO - Journal of Agricultural and Food Chemistry
JF - Journal of Agricultural and Food Chemistry
SN - 0021-8561
IS - 11
ER -