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Food Chem. 2017 Jan 1;214:393-399. doi: 10.1016/j.foodchem.2016.07.037. Epub 2016 Jul 6.

Changes in chemical interactions and protein conformation during heat-induced wheat gluten gel formation.

Author information

1
School of Food Science and Engineering, Hefei University of Technology, Hefei 230009, China.
2
School of Food Science and Engineering, Hefei University of Technology, Hefei 230009, China; Key Laboratory for Agricultural Products Processing of Anhui Province, Hefei 230009, China.
3
School of Food Science and Engineering, Hefei University of Technology, Hefei 230009, China; Key Laboratory for Agricultural Products Processing of Anhui Province, Hefei 230009, China. Electronic address: zhengzhi@hfut.edu.cn.

Abstract

In order to elucidate the heat-induced wheat gluten gel formation mechanism, changes in chemical interactions and protein conformation were investigated during gelation. The contribution of ionic and hydrogen bonds were found to decrease from 0.746 and 4.133g/L to 0.397 and 2.733g/L, respectively, as the temperature increased from 25 to 90°C. Moreover, the free SH content remarkably decreased from 37.91 to 19.79μmol/g during gelation. Ultraviolet absorption spectra and intrinsic fluorescence spectra suggested that wheat gluten unfolded during the heating process. In addition, wheat gluten gels treated at 80 and 90°C exhibited a "steric hindrance" effect, which can be attributed to the formation of aggregates. Fourier transform infrared spectra suggested that the random coil content increased at low temperatures (40 and 50°C), whereas the content of intermolecular β-sheets due to protein aggregation increased from 38.10% to 44.28% when the gelation temperature was 90°C.

KEYWORDS:

Chemical interaction; Dynamic rheological; Gel formation; Heat-induced; Network structure; Thermal aggregation; Wheat gluten

PMID:
27507490
DOI:
10.1016/j.foodchem.2016.07.037
[Indexed for MEDLINE]

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