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Effect of temperature, time and wheat gluten moisture content on wheat gluten network formation during thermomolding
- Jansens, Koen J.A., Lagrain, Bert, Rombouts, Ine, Brijs, Kristof, Smet, Mario, Delcour, Jan A.
- Journal of cereal science 2011 v.54 no.3 pp. 434-441
- crosslinking, cystine, disulfide bonds, gliadin, glutenins, temperature, water content, wheat gluten, wheat protein
- A plastic-like material can be obtained by thermomolding wheat gluten protein which consists of glutenin and gliadin. We studied the effect of molding temperature (130â170Â Â°C), molding time (5â25Â min) and initial wheat gluten moisture content (5.6â18.0%) on the gluten network. Almost no glutenins were extractable after thermomolding irrespective of the molding conditions. At the lowest molding temperature, the extractable gliadin content decreased with increasing molding times and moisture contents. This effect was more pronounced for the Î±- and Î³-gliadins than for the Ï-gliadins. Protein extractabilities under reducing conditions revealed that, at this molding temperature, the cross-linking was predominantly based on disulfide bonds. At higher molding temperatures, also non-disulfide bonds contributed to the gluten network. Decreasing cystine contents and increasing free sulfhydryl and dehydroalanine (DHA) contents with increasing molding temperatures and times revealed the occurrence of Î²-elimination reactions during thermomolding. Under the experimental conditions, the DHA derived cross-link lanthionine (LAN) was detected in all gluten samples thermomolded at 150 and 170Â Â°C. LAN was also formed at 130Â Â°C for gluten samples containing 18.0% moisture. Degradation was observed at 150Â Â°C for samples thermomolded from gluten with 18.0% moisture content or thermomolded at 170Â Â°C for all moisture contents.