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2021
DOI: 10.1016/j.foodhyd.2020.106285
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Less is more: Limited fractionation yields stronger gels for pea proteins

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Cited by 77 publications
(62 citation statements)
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References 35 publications
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“…In contrast to earlier findings, however, in this study, no evidence was found that the gel characteristics of 80% and 100% washed SPC gels were more prominent than others. A possible explanation might be that the higher gel strength was within the small deformation range, and correlated to the displacement of protein aggregates or other components, while the gel characteristics were determined within the large deformation range, referring to the disruption of a gel network [ 68 ].…”
Section: Resultsmentioning
confidence: 99%
“…In contrast to earlier findings, however, in this study, no evidence was found that the gel characteristics of 80% and 100% washed SPC gels were more prominent than others. A possible explanation might be that the higher gel strength was within the small deformation range, and correlated to the displacement of protein aggregates or other components, while the gel characteristics were determined within the large deformation range, referring to the disruption of a gel network [ 68 ].…”
Section: Resultsmentioning
confidence: 99%
“…Of these methods, AE‐IP is the most frequently used approach to isolate proteins (Chéreau et al., 2016; Vatansever et al., 2020). The AE‐IP protein isolation method utilizes some of the unique properties of pea proteins, such as their solubility at high pH and precipitation at their isoelectric point (Barac et al., 2010; Boye, Aksay et al., 2010; Boye, Zare et al., 2010; Cui et al., 2020; Kornet et al., 2021; Lan et al., 2018; O’Kane et al., 2005; Sridharan et al., 2020; Stone et al., 2015). The AE‐IP protein isolation technique typically involves three processes: (a) protein extraction at a higher pH level (8.0–9.5) and separating protein‐rich supernatant by centrifugation, (b) protein precipitation at an isoelectric point (pH 4.5–4.8) and separating the protein pellet by centrifugation, and (c) drying of the resulting protein isolates using freeze or spray drying (Table 3).…”
Section: Functional Properties Of Proteinmentioning
confidence: 99%
“…Most of the work done in the past decades has focused on protein isolates (80–95% protein) to assess pea protein functionality. However, recent studies suggest that high degree of purification is unnecessary to benefit from pea protein functionality [ 7 ] and that less-processed ingredients yield stronger heat-induced gel structures [ 8 ]. Nevertheless, in fermented pea protein gels, pasteurizing the matrix before fermentation is necessary to ensure safety and unique growth of the inoculated starter culture.…”
Section: Introductionmentioning
confidence: 99%