In this study, water-extractable arabinoxylan, WEAX, of wheat was isolated and mixed with gluten to observe small and large strain behavior and microscopic structure of the mixtures. The results showed that WEAX improves the viscoelasticity of gluten and makes the microscopic structure of gluten less compact. Free sulfhydryl, fluorescence anisotropy and CP/MAS 13C NMR measurements were used to gain a better understanding of the interactions between WEAX and gluten proteins of wheat. It was demonstrated that when gluten was mixed with WEAX, the free –SH of gluten proteins cross-linked to each other or to WEAX. The cross-linking happened mainly to LMW-GS. It was shown from the fluorescence anisotropy that the conformation of glutenin was more greatly influenced by WEAX than gliadin because of the difference in their molecular conformation. In addition, it was found in this study that tyrosine groups of glutenin also played an important role in the interactions between WEAX and gluten.
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Special thanks to Mr. Kongying, Zhu, Analysis and Test Center, the University of Tianjin, for his assistance in CP/MAS 13C NMR measurement of the samples used in this study. And also special thanks to Miss. Ren Wei, Liaoning University of Traditional Chinese Medicine, for her kind assistance in reviewing and amending an earlier manuscript. This work was supported by the National Natural Science Foundation of China under Grant No. 31440068 and by Science Technology Department of Zhejiang Province under Grant No. 2014C02023.
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This article does not contain any studies with human or animal subjects.
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