2004
DOI: 10.1016/j.jcis.2003.10.028
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Emulsifying properties of acylated rapeseed (Brassica napus L.) peptides

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Cited by 20 publications
(20 citation statements)
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“…2b). These values are close to those mentioned for acylated rapeseed peptides at air-water interface (Sánchez-Vioque et al 2004). The values indicate that introduction of maleyl groups facilitated flexibility of the protein molecule by exposing previously buried hydrophobic portions to the interface, thus enhancing lowering of surface tension (Lawal and Dawodu 2007) and such samples are expected to show improved foamability (Jain et al 2015).…”
Section: Surface Tensionsupporting
confidence: 84%
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“…2b). These values are close to those mentioned for acylated rapeseed peptides at air-water interface (Sánchez-Vioque et al 2004). The values indicate that introduction of maleyl groups facilitated flexibility of the protein molecule by exposing previously buried hydrophobic portions to the interface, thus enhancing lowering of surface tension (Lawal and Dawodu 2007) and such samples are expected to show improved foamability (Jain et al 2015).…”
Section: Surface Tensionsupporting
confidence: 84%
“…2b). This value was however found to be much lower than that reported for BSA (57.7 mN/m) (Sánchez-Vioque et al 2004), which points to the good adsorptive behavior and low surface tension of rapeseed protein at the air-water interface. Highly surface-active molecules were obtained by maleylation, the surface tension decreasing up to 36.9, 36 and 35.2 mN/m for 0.1MA, 0.2MA and 0.4MA, respectively (Fig.…”
Section: Surface Tensioncontrasting
confidence: 71%
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“…In fact, a longer, more hydrophobic chain results in a lower surface tension. This is attributed to the increase of the affinity of lipophilic molecules for interfaces [35].…”
Section: Critical Micellar Concentrationmentioning
confidence: 99%