Abstract
The effect of temperature (25, 45, and 65 °C) on the gluten secondary structure was investigated by using Fourier transform infrared (FTIR) spectroscopy and modulation of disulfide and hydrogen bonds contributions (100 ppm ascorbic acid (AA), 0.6% diacetyl tartaric acid ester of monoglycerides (DATEM), and 0.25 mM dithiothreitol (DTT)). The results showed that additives heated at 65 °C altered most of the gluten matrix formation by changing structural secondary structures compared to the secondary structures of native gluten (control). The content of random coils, α-helices, and β-sheet of gluten increased, while the extent of β-turns and antiparallel β-sheets decreased, which led to the transformation to a more stable secondary conformation. In addition, the rheological properties (%creep strain) revealed that gluten deformation increased during the heating process with all of the additives. The chemometric method could quantitate an overall alteration of gluten polymerization and gluten matrix formation during heating with additive treatments.
Highlights
As one of the largest biopolymers in nature, the gluten protein is a complex system with multi‐components and specific aggregation properties
We investigated the effect of temperature and additives on the secondary structure of gluten using Fourier transform infrared (FTIR)
Amide I vibrational band absorbs in the range of 1600–1700 cm−1, occurred mainly from C=O stretching vibration. This amide I vibration is normally applied for the study of protein backbone structure which is related to spectrum and secondary structure measurement
Summary
As one of the largest biopolymers in nature, the gluten protein is a complex system with multi‐components and specific aggregation properties. The intermolecular bonding of glutenin was applied to group the gluten structure into repetitive domains (spiral structure by β‐turn) and non‐repetitive domains (α‐helices structure and other cysteine residues). Hydrogen bonding could impact the second‐ ary structure of gluten. The cysteines in the C‐terminal domain of α‐ and β‐ gliadins and ω‐gliadins provide three and four homologous intrachain disulfide bonds of gliadin, re‐ spectively [1,2,3,4,5,6,7,8]. Monomeric gliadin protein with a low molecular weight (28–50 kDa) and S‐poor ω‐type does not provide elastic properties
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