2022
DOI: 10.1016/j.foodchem.2022.133109
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Effect of chemical structure of selected phenolic acids on the structure of gluten proteins

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Cited by 25 publications
(12 citation statements)
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“…The reduction of this phenolic compound in the JPS extracts after 60 min demonstrates that certain phenolic compounds interact with other components in the extracts and negatively affect their recovery as free phenolics. Previous reports indicate that hydroxybenzoic acids, depending on their structure, may be incorporated between peptide chains and aggregates . Carbohydrates may also be involved in aggregate formation with phenolic compounds .…”
Section: Results and Discussionmentioning
confidence: 99%
See 1 more Smart Citation
“…The reduction of this phenolic compound in the JPS extracts after 60 min demonstrates that certain phenolic compounds interact with other components in the extracts and negatively affect their recovery as free phenolics. Previous reports indicate that hydroxybenzoic acids, depending on their structure, may be incorporated between peptide chains and aggregates . Carbohydrates may also be involved in aggregate formation with phenolic compounds .…”
Section: Results and Discussionmentioning
confidence: 99%
“…Previous reports indicate that hydroxybenzoic acids, depending on their structure, may be incorporated between peptide chains and aggregates. 29 Carbohydrates may also be involved in aggregate formation with phenolic compounds. 30 Therefore, even if cellulase degraded JPS, the released compounds would form insoluble aggregates that could affect the total phenolics quantification.…”
Section: Total Phenolic Contents and The Quantification Of The Most A...mentioning
confidence: 99%
“…This may be related to the O'EN-F, a rich source of total phenolics and antioxidants that can form proteinpolyphenol interactions, which involve incorporating phenolic compounds into the gluten network and closing them in the hydrophobic pockets. 28 According to Welc et al, 29 these interactions can lead to structural and functional changes in gluten proteins, such as aggregation and altering the conformation of disulfide bridges. Danno and Hoseney 30 and Okada et al 31 have investigated free radical scavengers such as phenolic acids that can accelerate dough breakdown.…”
Section: Resultsmentioning
confidence: 99%
“…Notably, the EAI of US-GLE was improved by 6.35 m 2 /g compared to GLE. Welc et al [ 47 ] reported that phenolics could cut the intra-strand disulfide bonds, which maintain the conformational stability of proteins, thus conferring a more flexible spatial structure. Moreover, ultrasound treatment can also break the intra-strand disulfide bond of GL.…”
Section: Resultsmentioning
confidence: 99%