Abstract
A method for the preparation of soft capsules (Gl.C) and chewable gums (GCG) of the hydrophobic wheat protein, crude gliadin, is reported. Gliadin films were found to be more hydrophilic than comparable gelatin films. The release of paracetamol was significantly sustained, indicating drug delivery. Drug release profiles in 0.1 M hydrochloric acid media consisted of three regions for Gl.C: these were an initial latency period, followed by a low release region and essentially constant rate; and one region for GCG with very slow release of paracetamol. A mechanism of drug release is proposed involving hydrophobic interaction between gliadin and non-polar ligands. These results are discussed and based on this study, gliadin appears to be a highly promising, low-cost, bioacceptable protein for the manufacture of drug formulations with a very interesting controlled released potency.
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