Decoupling diffusion and macromolecular relaxation in the release of vitamin B6 from genipin-crosslinked whey protein networks.

This study examined the release of vitamin B6 from a hydrogel made of whey protein isolate (WPI). Work was carried out at ambient temperature without preheating the whey protein. Native-state macromolecules were crosslinked with a nontoxic compound, genipin. Experimentation included a ninhydrin assay with UV-vis absorbance, FTIR, C NMR, compression testing, SEM imaging, WPI matrix swelling and vitamin release protocols. It was confirmed that geninin crosslinked effectively the protein chains whose network strength was reinforced with increasing crosslinker concentrations. The modified Flory-Rehner theory predicted the molecular weight between crosslinks, network mesh size and crosslinking density in the swollen WPI gels as a function of added crosslinker. Transport patterns of vitamin B6 through the polymeric matrix were monitored over prolonged periods of observation. These were examined with the generalised Fick's equation and the Peppas-Sahlin equation to unveil the interplay between diffusion and relaxation dynamics in the anomalous transport of the bioactive compound.