Dilational rheology of protein films adsorbed at fluid interfaces

Lucassen-Reynders, E. H.; Benjamins, J.; Fainerman, V. B.

doi:10.1016/j.cocis.2010.05.002

Cited by 107 publications

(92 citation statements)

References 31 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Among the proteins present in Na-CAS, b-casein tends to dominate on the interface due to its increased surface activity (Jourdain et al, 2009). However, due to its increased flexibility, almost two fold higher than globular proteins, this protein component tends to generate interfaces with a low dilatational modulus (Lucassen-Reynders, Benjamins, & Fainerman, 2010). The presence of chitosan at the interfaces did not affect the rheological properties of the adsorbed biopolymer films (Fig.…”

Section: Adsorption Of Sodium Caseinate/chitosan Complexes At Oil/ Wamentioning

confidence: 95%

Properties of emulsions stabilised by sodium caseinate–chitosan complexes

Zinoviadou

Scholten

Moschakis

et al. 2012

International Dairy Journal

View full text Add to dashboard Cite

Section: Adsorption Of Sodium Caseinate/chitosan Complexes At Oil/ Wamentioning

confidence: 95%

Properties of emulsions stabilised by sodium caseinate–chitosan complexes

Zinoviadou

Scholten

Moschakis

et al. 2012

International Dairy Journal

View full text Add to dashboard Cite

“…2b) could be attributable to a restructuring and rearrangement of the interface protein with modification of the relaxation mechanisms that take place at an interface level, which contributes to greater elasticity of the film (Fig. 3) [27]. Moreover, the contribution of increased protein-protein interaction cannot be ruled out.…”

Section: Interfacial Viscoelasticitymentioning

confidence: 96%

Amaranth proteins foaming properties: Film rheology and foam stability – Part 2

Bolontrade

Scilingo

Añón

2016

Colloids and Surfaces B: Biointerfaces

View full text Add to dashboard Cite

In this work the influence of pH and ionic strength on the stability of foams prepared with amaranth protein isolate was analyzed. The behaviour observed was related to the physico-chemical and structural changes undergone by amaranth protein as a result of those treatments. The results obtained show that foams prepared at acidic pH were more stable than the corresponding to alkaline pH. At pH 2.0 the foams presented higher times and more volumes of drainage. This behaviour is consistent with the characteristics of the interfacial film, which showed a higher viscoelasticity and a greater flexibility at acidic pH than alkaline pH value, which in turn increased by increasing the concentration of proteins in the foaming solution. It is also important to note that the presence of insoluble protein is not necessarily detrimental to the properties of the foam. Detected changes in the characteristics of the interfacial film as in the foam stability have been attributed to the increased unfolding, greater flexibility and net charge of amaranth proteins at acidic conditions.

show abstract

“…b-Lactoglobulin (BLG), and proteins in general, readily adsorb at fluid interfaces forming a visco-elastic network [1][2][3][4][5]. Concerning the influence of the hydrophobic phase, the adsorption is more intensive at the water/oil interface compared to the water/air (W/ A) surface leading to smaller molar areas [1][2][3][4][5][6][7][8].…”

Section: Introductionmentioning

confidence: 99%

“…Concerning the influence of the hydrophobic phase, the adsorption is more intensive at the water/oil interface compared to the water/air (W/ A) surface leading to smaller molar areas [1][2][3][4][5][6][7][8]. This fact is attributed to the stronger cohesive interaction between the organic molecules and the protein's hydrophobic segments which leads to penetration of such segments into the oil phase thus changing the conformation of the protein in the adsorbed state compared to that at the W/A surface.…”

Section: Introductionmentioning

confidence: 99%