2023
DOI: 10.1016/j.ifset.2022.103248
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Investigation of novel cold atmospheric plasma sources and their impact on the structural and functional characteristics of pea protein

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Cited by 17 publications
(8 citation statements)
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“…Improvement in the gel strength following the TGase modification was also reported for the SPI and cPPI [70,71]. In the TGase-modified isolates, the relatively high-molecular-weight polymers (Figure 1) and lower % distribution of functional proteins (Figure 2 and Table 1) potentially contributed to the stronger protein-network formation [24]. In addition, the high relative abundance of intermolecular β-sheet and β-turn structures (Figure 3 and Table 3) contributed to the enhanced gel strength [24,[56][57][58][59], mostly facilitated by hydrogen bonding [32,50,72].…”
Section: Gel Strengthsupporting
confidence: 53%
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“…Improvement in the gel strength following the TGase modification was also reported for the SPI and cPPI [70,71]. In the TGase-modified isolates, the relatively high-molecular-weight polymers (Figure 1) and lower % distribution of functional proteins (Figure 2 and Table 1) potentially contributed to the stronger protein-network formation [24]. In addition, the high relative abundance of intermolecular β-sheet and β-turn structures (Figure 3 and Table 3) contributed to the enhanced gel strength [24,[56][57][58][59], mostly facilitated by hydrogen bonding [32,50,72].…”
Section: Gel Strengthsupporting
confidence: 53%
“…While there were some statistical differences in the surface charge among all tested samples, the values were not much different numerically (Table 2), except for that of the cSPI, which was evaluated as a reference. The slightly higher surface charge of the ChPI Inter-and intramolecular β-sheet structures have been associated with the enhanced gel strength of different proteins [24,[56][57][58][59]. In addition, Zhang et al [7] confirmed the importance of β-sheet structures to the formation of fibrous textures during the highmoisture extrusion of soy and gluten proteins for meat analog applications.…”
Section: Protein Surface Propertiesmentioning
confidence: 99%
“…Additionally, cold plasma modification can cause carbonylation and the cleaving of protein backbone peptide bonds. Bu et al investigated the effect of cold plasma treatment on the structure and functionality of pea protein [ 109 ]. It was found that cold plasma modification increased the surface hydrophobicity of the protein and resulted in the formation of soluble aggregates through disulfide linkages.…”
Section: Modification Strategies Of Pulse Protein Isolatesmentioning
confidence: 99%
“…It was found that cold plasma modification increased the surface hydrophobicity of the protein and resulted in the formation of soluble aggregates through disulfide linkages. Altered protein secondary structures contribute to significant enhancements in gelation and emulsification properties [ 109 ].…”
Section: Modification Strategies Of Pulse Protein Isolatesmentioning
confidence: 99%
“…Many authors studied plasma-activated water [28][29][30] for improved seed properties. Positive effects of cold plasma treatment on seed germination and seedling growth were observed for many types of seed, for example, maize [31,32] pea [24,33] and wheat [34][35][36].…”
Section: Introductionmentioning
confidence: 99%