2013
DOI: 10.1016/j.lwt.2012.06.002
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Functional, conformational and topographical changes of succinic acid deamidated wheat gluten upon freeze- and spray-drying: A comparative study

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Cited by 38 publications
(20 citation statements)
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“…A category-based analysis of the peak shape of infrared spectrum was conducted as Table 5. Table 5 showed that the control contained 42.46 % β-sheet, 17.69 % α-helix, 10.31 % β-turn and these were in an agreement with the reports of Liao Li et al [31] and Sun et al [33]. CFU pretreatment led to a significant change of the wheat gluten.…”
Section: Ftir Spectroscopic Characterizationsupporting
confidence: 89%
See 1 more Smart Citation
“…A category-based analysis of the peak shape of infrared spectrum was conducted as Table 5. Table 5 showed that the control contained 42.46 % β-sheet, 17.69 % α-helix, 10.31 % β-turn and these were in an agreement with the reports of Liao Li et al [31] and Sun et al [33]. CFU pretreatment led to a significant change of the wheat gluten.…”
Section: Ftir Spectroscopic Characterizationsupporting
confidence: 89%
“…It was observed that the contents of the secondary structure elements by analyzing the Amide I band of WG which had been resolved by deconvolution and secondary derivation and Gaussian curve fitting. The different Amide I regions were assigned to protein secondary structures according to previous reports, β-sheet, which contained intermolecular β-sheet of protein aggregation (1605-1615 cm −1 ), intra-molecular β-sheet (1615-1640 cm −1 ), anti-parallel β-sheet (1690-1700 cm −1 ), random coil (1640-1650 cm −1 ), α-helix (1650-1660 cm −1 ), β-turn (1675-1690 cm −1 ) [30][31][32]. A category-based analysis of the peak shape of infrared spectrum was conducted as Table 5.…”
Section: Ftir Spectroscopic Characterizationmentioning
confidence: 99%
“…Circular dichroism technology was used to determine the secondary structure of SPI (Liao, Wang, & Zhao, 2013). The CD spectra were recorded in the far UV range (250-190 nm) with a spectropolarimeter (Jasco J-815, Jasco Corp., Tokyo, Japan) at 20°C; a quartz cuvette was 10 mm optical path length; an interval of 0.2 nm and scan speed of 100 nm/min were used.…”
Section: Circular Dichroism (Cd) Analysismentioning
confidence: 99%
“…The silkworm protein hydrolysate was first pre-frozen at −80 °C on Petri dishes for 3 h. Then, the samples were freeze-dried without heating under 0.07 mPa vacuum (condenser temperature of −60 °C) for 24 h [14]. The dried mixture was obtained and referred as SPPH-f.…”
Section: Preparation Of Silkworm Pupae Protein Hydrolysatesmentioning
confidence: 99%