Impact of proteins–κ-carrageenan interactions on foam properties

Carp, D.J.; Baeza, Rosa; Bartholomai, G.B.; Pilosof, Ana M.R.

doi:10.1016/j.lwt.2003.11.007

Cited by 35 publications

(22 citation statements)

References 28 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Ganzevles et al [46 • ] have nicely illustrated how complex formation between β-lactoglobulin and pectin can slow down protein adsorption and reduce foam formation, though the precise effects are also dependent on the protein-polysaccharide ratio. On the other hand, Carp et al [47] have illustrated that interactions between protein and polysaccharide that enhance the gelation of the aqueous phase may aid foam stability through a reduction in drainage of liquid from the foam. A general review of protein-polysaccharide interactions in the bulk has been provided by Benichou et al [48 • ].…”

Section: Protein Adsorptionmentioning

confidence: 99%

Stabilization of bubbles and foams

Murray

2007

Current Opinion in Colloid & Interface Science

287

174

View full text Add to dashboard Cite

Section: Protein Adsorptionmentioning

confidence: 99%

Stabilization of bubbles and foams

Murray

2007

Current Opinion in Colloid & Interface Science

287

174

View full text Add to dashboard Cite

“…Previous studies on the effect of polysaccharides on foaming properties of food proteins have shown that foam stability is strongly increased [14].…”

Section: Introductionmentioning

confidence: 97%

Foaming properties of protein/pectin electrostatic complexes and foam structure at nanoscale

Schmidt

Novalès

Boué

et al. 2010

Journal of Colloid and Interface Science

View full text Add to dashboard Cite

The foaming properties, foaming capacity and foam stability, of soluble complexes of pectin and a globular protein, napin, have been investigated with a "Foamscan" apparatus. Complementary, we also used SANS with a recent method consisting in an analogy between the SANS by foams and the neutron reflectivity of films to measure in situ film thickness of foams. The effect of ionic strength, of protein concentration and of charge density of the pectin has been analysed. Whereas the foam stability is improved for samples containing soluble complexes, no effect has been noticed on the foam film thickness, which is almost around 315Å whatever the samples. These results let us specify the role of each specie in the mixture: free proteins contribute to the foaming capacity, provided the initial free protein content in the bulk is sufficient to allow the foam formation, and soluble complexes slow down the drainage by their presence in the Plateau borders, which finally results in the stabilisation of foams.

show abstract

“…At the beginning of the adsorption, WPC‐λC soluble complex showed lower diffusion rate; however, due to high elasticity of adsorbed film, the foamability of WPC‐λC was improved compared with pure WPC (Perez and others ). On the other hand, high viscosity effect of polysaccharides can hinder the air incorporation process (Carp and others ; ErÇElebi and IbanoĞLu ) and may result in reduced protein diffusion rate which limits the foamability (Baeza and others ).…”

Section: Introductionmentioning

confidence: 99%

Foaming Properties of Whey Protein Isolate and λ‐Carrageenan Mixed Systems

Wang

Zhang

Vardhanabhuti

2015

Journal of Food Science

View full text Add to dashboard Cite

Heating protein with polysaccharide under neutral or near neutral pH can induce the formation of soluble complex with improved functional properties. The objective of our research was to investigate the effects of λ-carrageenan (λC) concentrations and pH on foaming properties of heated whey protein isolate (WPI) and λC soluble complex (h-cpx) in comparison to heated WPI with added λC (pWPI-λC), and unheated WPI with λC (WPI-λC). In all 3 WPI-λC systems at pH 7, increasing λC concentration led to improved foamability until a certain concentration before it decreased. Despite their higher viscosity, both heated systems (pWPI-λC and h-cpx) showed significantly better foamability and foam stability compared to WPI-λC. Rheological results of foams with 0.25% λC suggested that higher elasticity and viscous films were produced in h-cpx and pWPI-λC systems corresponding to better foam stability. Foam microstructure images indicated that foams produced from h-cpx had thicker film and consisted of smaller initial bubble area and more uniform bubble size. Results from the effect of pH (6.2, 6.5, and 7.0) further confirmed that stronger interactions between WPI and λC during heating contributed to the improved foaming properties. Foam stability was higher in h-cpx system at all 3 pH levels, especially under pH 6.2 where there were strongest interactions between the biopolymers.

show abstract

Impact of proteins–κ-carrageenan interactions on foam properties

Cited by 35 publications

References 28 publications

Stabilization of bubbles and foams

Stabilization of bubbles and foams

Foaming properties of protein/pectin electrostatic complexes and foam structure at nanoscale

Foaming Properties of Whey Protein Isolate and λ‐Carrageenan Mixed Systems

Contact Info

Product

Resources

About