Abstract
Nowadays, consumers demand dietary fibre-enriched products of appropriate taste, texture, smell and appearance. Unfortunately, addition of the dietary fibre supplements to bread significantly reduces its quality which is connected with changes in the structure of gluten proteins. Structural changes as well as changes in the water state of gluten matrix induced by eight dietary fibres were observed by using Fourier transform infrared spectroscopy. To facilitate this the difference spectra were calculated by subtraction of the control (gluten only) infrared spectrum from the spectra of gluten-fibre mixtures. The presence of positive bands at ca. 1597 and 1235 cm−1 indicated aggregation of gluten proteins into hydrogen bonded β-sheets. These β-sheets can be formed by other β-sheets, antiparallel-β-sheets, β-turns and/or α-helices. The aggregation is probably induced by partial dehydration of gluten matrix due to competition for water molecules between gluten proteins and fibre polysaccharides. This assumption is confirmed by the presence of the negative band at 3237 cm−1 and decrease in the intensity of the band at 3051 cm−1. These bands are assigned to the weak and strong H-bonds in the gluten matrix, respectively. The results indicated that both weak and strong H-bonds are necessary to dough formation of adequate rheological properties.
Published Version
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