Abstract
Wheat bran arabinoxylan (WBAX) gels entrapping standard model proteins at different mass ratios were formed. The entrapment of protein affected the gel elasticity and viscosity values, which decreased from 177 to 138 Pa. The presence of protein did not modify the covalent cross-links content of the gel. The distribution of protein through the network was investigated by confocal laser scanning microscopy. In mixed gels, protein aggregates forming clusters were detected at protein/polysaccharide ratios higher than 0.25. These clusters were not homogeneously distributed, suggesting that WBAX and protein are located in two different phases. The apparent diffusion coefficient (Dm) of proteins during release from mixed gels was investigated for mass ratios of 0.06 and 0.12. For insulin, Dm increased significantly from 2.64 × 10−7 to 3.20 × 10−7 cm2/s as the mass ratio augmented from 0.06 to 0.12. No significant difference was found for Dm values of ovalbumin and bovine serum albumin released from the mixed gels. The results indicate that homogeneous protein/WBAX gels can be formed at low mass ratios, allowing the estimation of Dm by using an analytical solution of the second Fick’s law.
Highlights
Gels are polymeric three-dimensional networks, which swell on contact with water but do not dissolve [1]
The standard proteins used as a model in this study did not have any negative effect on the rheological and microstructural characteristics of protein/Wheat bran arabinoxylan (WBAX) gels at mass ratios of 0.06 and 0.12
At higher mass ratios (0.25, 0.5 and 1.0) the storage modulus of the mixed gels decreased by 20%, presenting proteins and polysaccharide located in two different phases
Summary
Gels are polymeric three-dimensional networks, which swell on contact with water but do not dissolve [1]. Oral delivery of proteins remains to be a very active area of research as proteins are an important class of therapeutic agents and the oral route is the most widely accepted means of administration. It is not feasible for direct delivery of protein drugs. Ferulated AX can make gels by covalent cross-linking of FA groups after oxidation by some chemical or enzymatic (laccase and peroxidase/H2O2 system) free radical-generating agents [12,13,14,15]. Diferulic acid (di-FA) and tri-ferulic acid (tri-FA) [16,17,18,19] have been identified as covalently cross-linked structures in AX gel. The protein release capacity of mixed gels was investigated
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