Journal
BIOMACROMOLECULES
Volume 9, Issue 2, Pages 568-573Publisher
AMER CHEMICAL SOC
DOI: 10.1021/bm7011136
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The morphology of wheat protein (WG) blends with polyvinyl alcohol (PVA) and respectively with thiolated polyvinyl alcohol (TPVA) was investigated by atomic force (AFM) and transmission electron microscopy (TEM) as well as by modulated dynamic scanning calorimetry (MDSC). Thiolated additives based on PVA and other substrates were previously presented as effective means of improving the strength and toughness of compression molded native WG bars via disulfide-sulfhydryl exchange reactions. Consistent with our earlier results, AFM and TEM imaging clearly indicate that the addition of just a few mole percent of thiol to PVA was sufficient to dramatically change its compatibility with wheat protein. Thus, TPVA is much more compatible with WG and phase separates into much smaller domains than in the case of PVA, although there are still two phases in the blend: one WG-rich phase and another TPVA-rich phase. The WG/TPVA blend has phase domains ranging in size from 0.01 to 0.1 mu m, which are roughly 10 times smaller than those of the WG/PVA blend. MDSC further illustrates the compatibilization of the protein with TPVA via the dependence of the transition temperatures on composition.
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