2002
DOI: 10.1016/s0141-8130(02)00041-7
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Dynamic light scattering investigation of sodium caseinate and xanthan mixtures

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Cited by 39 publications
(26 citation statements)
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“…59 However, for sodium caseinate-xanthan systems it has been reported that the mixtures corresponded to the superposition of the modes of the pure biopolymers, suggesting the absence of interactions between the components in the concentration range studied. 60 In this study, the sodium alginate/pectin system showed an increase in R H after stirring the solutions for 24 h at 25 °C and 80 °C, in either NaCl or KCl. A similar effect has been observed by Hiorth et al 12 for chitosan and high pectin content solutions.…”
Section: Dynamic Light Scattering Of Ternary Pectin and Alginate Mixtmentioning
confidence: 58%
“…59 However, for sodium caseinate-xanthan systems it has been reported that the mixtures corresponded to the superposition of the modes of the pure biopolymers, suggesting the absence of interactions between the components in the concentration range studied. 60 In this study, the sodium alginate/pectin system showed an increase in R H after stirring the solutions for 24 h at 25 °C and 80 °C, in either NaCl or KCl. A similar effect has been observed by Hiorth et al 12 for chitosan and high pectin content solutions.…”
Section: Dynamic Light Scattering Of Ternary Pectin and Alginate Mixtmentioning
confidence: 58%
“…Alternatively, it cannot be overruled that these particles are made of milk protein; particularly NaCAS particles are known to self associate through hydrophobic interactions. However, the NaCAS aggregates have been reported to be smaller than 100 nm (Chu, Zhou, Wu, & Farrell, 1995;Nash, Pinder, Hemar, & Singh, 2002) while the aggregates seen in Fig. 7A2 and B2 are in the m range.…”
Section: Confocal Microscopy Of Protein/rice Starch Granule Mixturesmentioning
confidence: 90%
“…Sodium caseinate has been characterised in aqueous solution using static and dynamic light scattering by a number a research groups [2][3][4][5][6][7][8]. Caseinate is present as individual molecules at low ionic strength (3 mM), but forms small aggregates with a z-average hydrodynamic radius (R hz ) of about 11 nm at neutral pH, room temperature and high ionic strength (>100 mM) [8,9].…”
Section: Introductionmentioning
confidence: 99%
“…Sodium caseinate solutions also contain a small weight fraction of larger particles with a radius of about 80 nm [2,6,8,9]. The nature of the larger particles is, as yet, unknown, but it is clear that they are not residual native casein since, contrary to the latter, they do not sediment during ultracentrifugation.…”
Section: Introductionmentioning
confidence: 99%