2023
DOI: 10.1111/1541-4337.13144
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Cold atmospheric plasma‐induced protein modification: Novel nonthermal processing technology to improve protein quality, functionality, and allergenicity reduction

Abstract: With the constant increase in protein demand globally, it is expedient to develop a strategy to effectively utilize protein, particularly those extracted from plant origin, which has been associated with low digestibility, poor techno-functional properties, and inherent allergenicity. Several thermal modification approaches have been developed to overcome these limitations and showed excellent results.Nevertheless, the excessive unfolding of the protein, aggregation of unfolded proteins, and irregular protein … Show more

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Cited by 25 publications
(6 citation statements)
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References 149 publications
(299 reference statements)
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“…Our results agreed with Zhang and his colleagues who noticed the enhanced concentration of soluble protein, in soybean after Ar-plasma treatment [ 51 ]. CAP-generated reactive species can break protein bonds and modify sulfur-containing amino acids, leading to structural changes, reduced enzyme activity, and increased solubility [ 52 ].…”
Section: Discussionmentioning
confidence: 99%
“…Our results agreed with Zhang and his colleagues who noticed the enhanced concentration of soluble protein, in soybean after Ar-plasma treatment [ 51 ]. CAP-generated reactive species can break protein bonds and modify sulfur-containing amino acids, leading to structural changes, reduced enzyme activity, and increased solubility [ 52 ].…”
Section: Discussionmentioning
confidence: 99%
“…According to Ding et al [169], high-hydrostatic-pressure processing can reduce the allergenicity of allergens through different mechanisms, such as protein denaturation, protein aggregation or crosslinking, and protein conformational changes, and it can also inactivate microorganisms. Cold atmospheric plasma-induced protein modification, enzymatic modification, and fermentation have also been shown to alleviate the allergenicity of plant proteins [170][171][172].…”
Section: Plant Proteinsmentioning
confidence: 99%
“…The aggregation may be promoted here via the increased hydrophobic interaction. Thus, the ARAVCP treatment seems to lead to more flexible structures without a strong network of disulfide bonds [70][71][72].…”
Section: Influence Of Vcp On the Aggregation Behavior And ζ-Potentialmentioning
confidence: 99%