Abstract
A thermally treated wheat gluten (TTG) was structurally modified by enzymatic hydrolysis. Hydrolysis was carried out using a fungal protease. The solubility of hydrolysates having low, medium and high degrees of hydrolysis (DH) and the foaming properties of their extracts at each pH were determined. For comparison, a sample of TTG was used as a standard. The results showed that solubility increased as the DH increased, but foaming properties began to be impaired beyond a certain DH. Therefore, a minimum protein structure has to be retained, in order to keep good foaming properties. Mild hydrolysis (DH 14%) not only permitted the solubilisation of gluten proteins in a bigger pH range, but at pHs 9 and 6.5, good foaming properties were also obtained, which gave us the chance to expand wheat gluten utilisation.
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