12 January - 20 June 2016

The addition of dietary fibre preparations induce changes in the structure of gluten proteins

21 October 2015

Interactions between gluten proteins and dietary fibre preparations are crucial in the baking industry. The addition of dietary fibre to bread causes significant reduction in its quality which is influenced by changes in the structure of gluten proteins. Wheat proteins include albumins, globulins, gliadins and glutenin, but only the last two participate in the formation of a continuous viscoelastic network within dough. The structure of both proteins is crucial in the breadmaking process, but is also connected with gluten allergenicity. Studies on limiting or eliminating allergenicity of gluten proteins by biochemical modifications have been carried out for several years. A considerable decrease in the gluten allergenicity was observed after treatment with transglutaminase, acetic acid or citric acid, causing deamination. Dietary fibre preparations rich in antioxidants can be regarded as good candidates for decreasing gluten allergenicity. 

In a recent Polish study published in the journal Food Chemistry, the dietary fibres used were chosen because of their different sources in origin, and hence different chemical composition. Due to their different chemical composition they could interact with gluten proteins in different ways causing changes in the protein structure. The objective of the study was to determine changes in secondary and tertiary structure of gluten proteins mixed directly with dietary fibre preparation without starch. Fourier transform Raman spectroscopy was applied to determine changes in the structure of gluten proteins modified by seven dietary fibres. The commercially available gluten proteins without starch were mixed with the fibres in three concentrations: 3%, 6% and 9%. The results obtained showed that all fibres, regardless of their origin, caused the same kind of changes. The results indicated that presence of cellulose was the probable cause of these changes, and lead to aggregation or abnormal folding of the gluten proteins.

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