Functional, nutritional and conformational changes from deamidation of wheat gluten with succinic acid and citric acid

Liao, Lan; Liu, Tongxun; Zhao, Ming; Cui, Chun; Yuan, Boen; Tang, Sheng; Yang, Fei

doi:10.1016/j.foodchem.2010.04.017

Cited by 67 publications

(60 citation statements)

References 22 publications

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“…Similar to the AgNP-treated samples, the FTIR spectra of the amide I band showed a slight shift of the absorption maximum from 1648 to 1645 cm -1 . This shift can be connected with cleavage of peptide bonds (Liao et al, 2010). The TC-treated gluten samples were composed of approximately 48.0% (±0.5%) of a-helices, 39.6% (±0.4%) of b-sheets, and 12.4% (±0.3%) of b-turns.…”

Section: Resultsmentioning

confidence: 94%

“…3a) indicated that the conformational changes were probably connected with cleavage of peptide bonds. Liao et al (2010) studied the influence of the process of gluten deamination by succinic acid and citric acid on the secondary structure of the protein. Changes in the percentage contribution of structural components were observed but there was no maximum shift.…”

Section: Resultsmentioning

confidence: 99%

“…Changes in the percentage contribution of structural components were observed but there was no maximum shift. Therefore, the conformational changes in gluten were mainly caused by increased electrostatic repulsion and a decrease in the number of hydrogen bonds (Liao et al, 2010). The changes in the secondary structure of the treated gluten were significant, therefore, the factors causing them should be found.…”

Section: Resultsmentioning

confidence: 99%

“…The absorbance maximum of the amide I band was not shifted after using water and was located at 1648 cm -1 . The zero shift of the amide I band maximum indicated that the secondary conformational changes were mainly caused by electrostatic interactions and a decrease in the number of hydrogen bonds (Liao et al, 2010). The percentage contribution of the structural components is shown in Table 1.…”

Section: Resultsmentioning

confidence: 99%

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Conformational Changes in Wheat Gluten After using Ag-nanoparticles

Nawrocka¹

2014

International Agrophysics

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A b s t r a c t. Silver nanoparticles have antimicrobial properties since they can be regarded as an efficient protector against pathogenic microorganisms. Fourier transform infrared spectroscopy was used to examine conformational changes in the secondary structure of wheat gluten washed out from grain treated with an aqueous solution of silver nanoparticles stabilized by trisodium citrate. Silver nanoparticles were used as a protective layer on the grain surface against bacterial and fungal infections (antimicrobial agent). Analysis of the amide I band revealed significant changes in the secondary structure after using silver nanoparticles. An increase in the b-sheet content (from 36.2 to 39.2%) was observed at the expense of the a-helix and b-turn content. To find factors causing these changes, the wheat grains were treated by an aqueous solution of trisodium citrate and water. The results obtained indicate that the changes in the gluten structure were connected mainly with the trisodium citrate action due to presence of a small number of free molecules of the stabilizer in the solution of silver nanoparticles. Additionally, the conformational changes in gluten pointed out that gluten flexibility increased (decrease in the aH/bS ratio from 1.40 for the control sample to 1.26 for the silver nanoparticle-treated samples) as well as the solubility of gluten decreased (decrease in the b-turn content from 13.1 to 11.4%).K e y w o r d s: silver nanoparticles, trisodium citrate, wheat gluten, FTIR spectroscopy, secondary structure

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Section: Resultsmentioning

confidence: 94%

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

See 2 more Smart Citations

Conformational Changes in Wheat Gluten After using Ag-nanoparticles

Nawrocka¹

2014

International Agrophysics

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“…A modification of its properties in a controlled way would facilitate the production of added value oat ingredients having good emulsifying and stabilizing properties in one package. It is known that deamidation of protein-rich raw materials of plant origin (e.g., wheat or corn gluten) improves emulsifying ability after chemical and enzymatic deamidation (Liao et al, 2010;Yong et al, 2004). Also, the emulsifying ability of oat proteins (mainly 11S globulins) can be improved by the treatment combining high temperature and mild acidity, which elicited deamidation of oat proteins (Ma and Khanzada, 1987).…”

Section: Introductionmentioning

confidence: 99%