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    Dynamic rheological behavior of wheat glutens during heating
    (John Wiley & Sons Ltd, 2005) Hayta, M; Schofield, JD
    Creep and dynamic rheological tests indicated that addition of redox additives directly into gluten or into flour before gluten extraction resulted in differences in rheological parameters. Heating from 30 to 50 degrees C caused a decrease in elastic modulus whereas heating above 50 degrees C strengthened the structure as evidenced by an increase in elastic modulus. Higher elastic modulus and lower creep compliance values suggested that Hereward gluten was more highly cross-linked than Riband gluten. Glutenin seemed to be affected more than gliadin during temperature sweep experiments. Both oxidising and reducing reagents showed similar weakening effects on gluten irrespective of addition into flour or gluten. Treatment with oxidising reagents, particularly bromate, slightly delayed the temperature for the increase in elastic modulus as assessed by temperature sweep experiments. The identical effect of reducing and oxidising reagents may be attributable to the differences in mode of action and intrinsic material properties. (c) 2005 Society of Chemical Industry.
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    Heat and additive induced biochemical transitions in gluten from good and poor breadmaking quality wheats
    (Academic Press Ltd Elsevier Science Ltd, 2004) Hayta, M; Schofield, JD
    Glutens from poor breadmaking quality wheat, cv. Riband, had a higher SDS extractability than glutens from good quality cv. Hereward. Heating of gluten, especially above 70 degreesC, caused a reduction in the amount of SDS-extractable gluten proteins. Treatment of gluten with redox additives (ascorbic acid, potassium bromate or glutathione) affected extractability, being highest for bromate treated glutens. The SH content of gluten was lower for poor breadmaking Riband and heating resulted in greater decrease in SH content of gluten from good breadmaking Hereward. Hereward gluten had a higher SS content than Riband. The alteration of SS content on heating was not significant and may indicate the heat-induced involvement of non-covalent interactions. SDS-PAGE revealed that oxidants, especially bromate, affect polypeptide composition leading to a more heat stable/tolerant protein structure. (C) 2004 Published by Elsevier Ltd.