Aging properties of films of plasticized vital wheat gluten cast from acidic and basic solutions
2006 (English)In: Biomacromolecules, ISSN 1525-7797, E-ISSN 1526-4602, Vol. 7, no 5, 1657-1664 p.Article in journal (Refereed) Published
In order to understand the mechanisms behind the undesired aging of films based on vital wheat gluten plasticized with glycerol, films cast from water/ethanol solutions were investigated. The effect of pH was studied by casting from solutions at pH 4 and pH 11. The films were aged for 120 days at 50% relative humidity and 23 C, and the tensile properties and oxygen and water vapor permeabilities were measured as a function of aging time. The changes in the protein structure were determined by infrared spectroscopy and size-exclusion and reverse-phase high-performance liquid chromatography, and the film structure was revealed by optical and scanning electron microscopy. The pH 11 film was mechanically more stable with time than the pH 4 film, the latter being initially very ductile but turning brittle toward the end of the aging period. The protein solubility and infrared spectroscopy measurements indicated that the protein structure of the pH 4 film was initially significantly less polymerized/ aggregated than that of the pH 11 film. The polymerization of the pH 4 film increased during storage but it did not reach the degree of aggregation of the pH 11 film. Reverse-phase chromatography indicated that the pH 11 films were to some extent deamidated and that this increased with aging. At the same time a large fraction of the aged pH 11 film was unaffected by reducing agents, suggesting that a time-induced isopeptide cross-linking had occurred. This isopeptide formation did not, however, change the overall degree of aggregation and consequently the mechanical properties of the film. During aging, the pH 4 films lost more mass than the pH 11 films mainly due to migration of glycerol but also due to some loss of volatile mass. Scanning electron and optical microscopy showed that the pH 11 film was more uniform in thickness and that the film structure was more homogeneous than that of the pH 4 film. The oxygen permeability was also lower for the pH 11 film. The fact that the pH 4 film experienced a larger and more rapid change in its mechanical properties with time than the pH 11 film, as a consequence of a greater loss of plasticizer, was presumably due to its initial lower degree of protein aggregation/ polymerization. Consequently, the cross-link density achieved at pH 4 was too low to effectively retain volatiles and glycerol within the matrix.
Place, publisher, year, edition, pages
2006. Vol. 7, no 5, 1657-1664 p.
hydrogen-ion equilibria, barrier properties, mechanical-properties, secondary structure, chemical properties, protein-composition, dope solution, transport, time, increase
IdentifiersURN: urn:nbn:se:kth:diva-14024DOI: 10.1021/bm0600973ISI: 000237593600036ScopusID: 2-s2.0-33744517880OAI: oai:DiVA.org:kth-14024DiVA: diva2:329163
QC 201007082010-07-082010-07-082010-11-03Bibliographically approved