2006
DOI: 10.1016/j.foodchem.2005.01.030
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Surface hydrophobicity of commercial canola proteins mixed with κ-carrageenan or guar gum

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Cited by 56 publications
(26 citation statements)
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“…In contrast, the surface hydrophobicity was increased at higher XG levels. A similar observation was reported in a canola protein isolate-carrageenan system by Uruakpa et al (Uruakpa & Arntfield, 2006), who suggested the surface hydrophobicity increased due to the exposure of hydrophobic residues in presence of strong electrostatic repulsive forces. Therefore, the larger repulsive forces in the mixed gel control the rate of protein aggregation, and hydrophobic groups were exposed during heating, which produced a sheet-like gel structure, leading to a poor gel texture and whiteness.…”
Section: Changes In T 2 Of Mixed Gels In Lf-nmr With Different Concsupporting
confidence: 84%
“…In contrast, the surface hydrophobicity was increased at higher XG levels. A similar observation was reported in a canola protein isolate-carrageenan system by Uruakpa et al (Uruakpa & Arntfield, 2006), who suggested the surface hydrophobicity increased due to the exposure of hydrophobic residues in presence of strong electrostatic repulsive forces. Therefore, the larger repulsive forces in the mixed gel control the rate of protein aggregation, and hydrophobic groups were exposed during heating, which produced a sheet-like gel structure, leading to a poor gel texture and whiteness.…”
Section: Changes In T 2 Of Mixed Gels In Lf-nmr With Different Concsupporting
confidence: 84%
“…Canola protein-hydrocolloid hybrid systems composed of up to 20% (w/w) protein (protein product had 87% protein that is composed of 3% of 2S protein and 97% of 11S(or 7S) protein and 3% (w/w) κ-carrageenan resulted in gels with improved strength and structure and provided more elasticity (Uruakpa and Arntfield, 2004) but guar gum produced less elastic gels (Uruakpa and Arntfield, 2005). Structure formation and stabilization of the polysaccharidecanola protein gels were mediated by hydrophobic, noncovalent and covalent interactions (Uruakpa and Arntfield, 2006). Canola napin can induce thermal aggregation of β-casein, which can be controlled by protein concentration, pH and salt level, and the napin aggregation was found thermoreversible (Schwartz et al, 2015).…”
Section: Gel Network Formationmentioning
confidence: 99%
“…However, there is very little information regarding hydrophobicity of CPI or the changes induced in aqueous environment, solvents, and proteolytic enzymes. Uruakpa and Arntfield (2006a) reported that surface hydrophobicity of CPI was affected by the presence of a hydrocolloid (guar gum, κ-carrageenan) that generally increased the hydrophobicity of CPI. This could possibly be due to the interaction between CPI and the hydrocolloid that enhanced protein unfolding, thus exposing the buried hydrophobic amino acid residues.…”
Section: Hydrophobicitymentioning
confidence: 99%