2017
DOI: 10.1016/j.foodchem.2017.03.114
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Structuring colloidal oat and faba bean protein particles via enzymatic modification

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Cited by 79 publications
(62 citation statements)
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“…Figure 1. The profile was quite similar to previously published SDS-PAGE results for faba bean protein [34,37,39]. The majority of proteins found in pulses are globulins (~70-78%), followed by albumins (10-20%) [1,40].…”
Section: Compositional Analysissupporting
confidence: 88%
See 1 more Smart Citation
“…Figure 1. The profile was quite similar to previously published SDS-PAGE results for faba bean protein [34,37,39]. The majority of proteins found in pulses are globulins (~70-78%), followed by albumins (10-20%) [1,40].…”
Section: Compositional Analysissupporting
confidence: 88%
“…Protein contents of similarly produced protein-rich fractions from peas are typically in the range of~50-60% (DM) [35,36]. On the other hand, aqueous processing allows for higher protein purity; faba bean and other legume protein isolates are often in the range of 80-90% or higher [12,37,38]. Fat content was higher in FPI than FPR, indicating that fat was concentrated to some extent as part of the isolation process.…”
Section: Compositional Analysismentioning
confidence: 99%
“…The presence of less hydrophobic sites and higher charge densities results in an increase in water solubility; in addition, high electrostatic repulsion and hydration of ions lead to enhanced protein solubility at pH values below and above its p I . Energies associated with interactions between biopolymer–biopolymer and biopolymer–solvent play a critical role in their solubility . Solubility of proteins at their isoelectric point (p I ) is higher when the protein is forming a complex with the polysaccharide than without .…”
Section: Functional Properties Of Protein–polysaccharide Complexesmentioning
confidence: 99%
“…54,[84][85][86][87] Energies associated with interactions between biopolymer-biopolymer and biopolymer-solvent play a critical role in their solubility. 54,88 Solubility of proteins at their isoelectric point (pI) is higher when the protein is forming a complex with the polysaccharide than without. 51,89 It has been identified that biopolymer mixing ratio is the factor most responsible for the solubility of proteins when they are in complexes 54 .…”
Section: Protein Solubilitymentioning
confidence: 99%
“…Potential food-compatible technologies for improving the functionality of cereal proteins include protein cross-linking by enzymatic means (18,37,40); shear-induced processing (e.g., microfluidization) (16); complexation with polysaccharides (19,21,33,53) or other proteins (22); and complete or limited hydrolysis by enzymatic means (62). The major challenges associated with hydrolysis methods is the off-flavor formation generated by peptides, and therefore, limited/controlled hydrolysis should be favored as an approach in many cases.…”
Section: Liquid and Semisolid Food Applicationsmentioning
confidence: 99%