“…Amide II (1500–1600 cm −1 ) and amide III (1100–1600 cm −1 ) bands corresponding to N–H bending and protein side chains chemical groups, respectively, are used to further substantiate analysis from amide I due to weak absorption of proteins at these bands, and data showed a maximum shift from 1588 to 1583 cm −1 , and 1141 to 1132 cm −1 , respectively. Overall, results showed a slight transition in the secondary structure of the protein from treatment and such changes were accompanied by improved biological properties of proteins in food model systems [66] .…”
Section: Resultsmentioning
confidence: 88%
“…Similar results have been reported for Atlantic salmon treated with acidic electrolyzed water [22] . FTIR is typically used to evaluate the secondary structure of proteins and the spectra region of 110–1700 cm −1 provides valuable information on protein polypeptide conformation [66] . Fig.…”
Section: Resultsmentioning
confidence: 99%
“…Furthermore, the maximum absorbance in the amide I band was at 1635 cm −1 for fresh grass carp and this shifted to 1630 and 1629 cm −1 , respectively, for individual and combination treatments, indicating a slight transition as a result of treatment. The amide I band located between 1600 and 1700 cm −1 typically indicates C = O stretching vibrations, C–C-N deformation, C-N stretch, in-plane bending, and is generally referred to as the fingerprint for protein secondary structure [66] . Spectral changes in this region have been associated with soy protein hydrolysates and salmon conformational changes as a result of ultrasound and electrolyzed water processing [22] , [66] .…”
Section: Resultsmentioning
confidence: 99%
“…The amide I band located between 1600 and 1700 cm −1 typically indicates C = O stretching vibrations, C–C-N deformation, C-N stretch, in-plane bending, and is generally referred to as the fingerprint for protein secondary structure [66] . Spectral changes in this region have been associated with soy protein hydrolysates and salmon conformational changes as a result of ultrasound and electrolyzed water processing [22] , [66] . Amide II (1500–1600 cm −1 ) and amide III (1100–1600 cm −1 ) bands corresponding to N–H bending and protein side chains chemical groups, respectively, are used to further substantiate analysis from amide I due to weak absorption of proteins at these bands, and data showed a maximum shift from 1588 to 1583 cm −1 , and 1141 to 1132 cm −1 , respectively.…”
“…Amide II (1500–1600 cm −1 ) and amide III (1100–1600 cm −1 ) bands corresponding to N–H bending and protein side chains chemical groups, respectively, are used to further substantiate analysis from amide I due to weak absorption of proteins at these bands, and data showed a maximum shift from 1588 to 1583 cm −1 , and 1141 to 1132 cm −1 , respectively. Overall, results showed a slight transition in the secondary structure of the protein from treatment and such changes were accompanied by improved biological properties of proteins in food model systems [66] .…”
Section: Resultsmentioning
confidence: 88%
“…Similar results have been reported for Atlantic salmon treated with acidic electrolyzed water [22] . FTIR is typically used to evaluate the secondary structure of proteins and the spectra region of 110–1700 cm −1 provides valuable information on protein polypeptide conformation [66] . Fig.…”
Section: Resultsmentioning
confidence: 99%
“…Furthermore, the maximum absorbance in the amide I band was at 1635 cm −1 for fresh grass carp and this shifted to 1630 and 1629 cm −1 , respectively, for individual and combination treatments, indicating a slight transition as a result of treatment. The amide I band located between 1600 and 1700 cm −1 typically indicates C = O stretching vibrations, C–C-N deformation, C-N stretch, in-plane bending, and is generally referred to as the fingerprint for protein secondary structure [66] . Spectral changes in this region have been associated with soy protein hydrolysates and salmon conformational changes as a result of ultrasound and electrolyzed water processing [22] , [66] .…”
Section: Resultsmentioning
confidence: 99%
“…The amide I band located between 1600 and 1700 cm −1 typically indicates C = O stretching vibrations, C–C-N deformation, C-N stretch, in-plane bending, and is generally referred to as the fingerprint for protein secondary structure [66] . Spectral changes in this region have been associated with soy protein hydrolysates and salmon conformational changes as a result of ultrasound and electrolyzed water processing [22] , [66] . Amide II (1500–1600 cm −1 ) and amide III (1100–1600 cm −1 ) bands corresponding to N–H bending and protein side chains chemical groups, respectively, are used to further substantiate analysis from amide I due to weak absorption of proteins at these bands, and data showed a maximum shift from 1588 to 1583 cm −1 , and 1141 to 1132 cm −1 , respectively.…”
“…The increase in intermolecular β-sheets further demonstrated that protein polymerized during heating of wheat flour. In order to obtain further information concerning protein structural changes, an intrinsic fluorescence spectroscopy was used to depict the alterations in protein tertiary structure [ 25 ]. The intrinsic fluorescence intensity reduced largely when the temperature exceeded 70 °C and reached its minimum at 100 °C.…”
The behaviors of starch and protein in wheat flour during heating were investigated, and the molecular changes of starch and protein and their effects on the textural characteristics were assessed. The results showed that with the increased temperature, soluble protein aggregated to insoluble high-molecular-weight protein polymers when the heating temperature exceeded 70 °C, and the aggregation of protein was mainly caused by covalent bonds of disulfide (SS) bonds. Hydrophobic interaction was the main noncovalent bond that participated in the formation of protein aggregates. The major change in the secondary structure during heating was a pronounced transition towards β-sheet-like structures. Considerable disruption of ordered structures of starch occurred at 70 °C, and starch was fully gelatinized at 80 °C. Typical starch pasting profiles of cooked flour were observed when the temperature was below 70 °C, and heat treatment decreased the pasting viscosity of the cooked flour from control to 80 °C, whereas the viscosity of the wheat flour increased in heating treatment at 90, 95 and 100 °C. The intense protein-starch interaction during heating affected the textural characteristic of flour gelation, which showed higher strength at 90, 95 and 100 °C. This study may provide a basis for improving wheat flour processing conditions and could lead to the production of new wheat products.
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