Mechanism and characteristics of protein release from lactitol-based cross-linked hydrogel

Jung H. Han, John M. Krochta, You Lo Hsieh, Mark J. Kurth

Research output: Contribution to journalArticle

19 Scopus citations

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 languageEnglish (US)
Pages (from-to)5658-5665
Number of pages8
JournalJournal of Agricultural and Food Chemistry
Volume48
Issue number11
DOIs
StatePublished - 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)

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