Effect of foaming temperature and varying time/temperature-conditions of pre-heating on the foaming properties of skimmed milk

Borcherding, K.; Lorenzen, Peter Christian; Hoffmann, Wolfgang; Schrader, Katrin

doi:10.1016/j.idairyj.2007.11.016

Cited by 51 publications

(38 citation statements)

References 34 publications

(35 reference statements)

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“…The enhanced interactions during the formation of h‐cpx likely increased the elasticity of the interfacial film, reduced the mobility of aqueous phase and slowed down the rates of bubble shrinkage or growth. Based on the analysis, the smaller initial bubble size of h‐cpx corresponded to better foam stability, which was in agreement with other studies (Borcherding and others ). Natural logarithm values of bubble areas were used to describe the bubble size distribution.…”

Section: Resultssupporting

confidence: 91%

“…Foams are colloidal systems formed by the agglomerations of dispersed phase (gas) in the continuous phase (Damodaran and Paraf ). Proteins, as amphiphilic macromolecules, are considered as foaming agent because they have the ability to unfold and adsorb at the interfaces between the dispersed and continuous phases (Borcherding and others ; Tamm and others ) and to form a viscoelastic adsorbed layer (Wilde ). Foaming properties of whey protein isolate (WPI) have been the subject of investigations.…”

Section: Introductionmentioning

confidence: 99%

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

Wang

Zhang

Vardhanabhuti

2015

Journal of Food Science

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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.

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Section: Resultssupporting

confidence: 91%

Section: Introductionmentioning

confidence: 99%

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

Wang

Zhang

Vardhanabhuti

2015

Journal of Food Science

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“…2-5). Decreasing surface tension -or a stronger affinity of milk protein molecules towards interfaces -theoretically (Borcherding, Lorenzen, Hoffmann, & Schrader, 2008) corresponds to increasing surface hydrophobicity values as diagrammed in Figs. 2-5.…”

Section: Techno-functional Properties Of Enzymatically Treated Milk Pmentioning

confidence: 94%

Functional properties of milk proteins as affected by enzymatic oligomerisation

Hiller¹,

Lorenzen²

2009

Food Research International

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“…However, if sufficient native protein is present, this can form fine foam bubbles which are stabilised more efficiently by the large protein aggregates. Various researchers [37][38][39][40] explain that foaming ability is guided by the surface tension and the rate of diffusion of particles onto the air-water interface. Particles that diffuse rapidly to the air-water interface and are able to reduce surface tension rapidly will stabilise the air bubbles in foam more quickly and will give rise to smaller bubbles and a greater foam volume.…”

Section: Foaming Abilitymentioning

confidence: 99%

Electrostatic complexes of whey protein and pectin as foaming and emulsifying agents

Oduse¹,

Campbell

Lonchamp

et al. 2017

International Journal of Food Properties

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Five types of electrostatic complex (macromolecular complexes, core-shell particles, and mixed homogeneous particles) were formed between whey protein (whey protein concentrate [WPC]) and pectin. By controlling the thermal treatment, composition, and order of mixing, it was possible to produce complexes that for the same biopolymer concentration gave differing functional properties. All protein-pectin complexes showed higher foaming ability and stability than native or heated WPC without pectin. Native WPC had higher emulsifying ability than protein-pectin complexes but exhibited the lowest emulsion stability. Ingredients based on such ideas might offer the food manufacturer greater control over food structure, stability, and organoleptic properties. ARTICLE HISTORY

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Effect of foaming temperature and varying time/temperature-conditions of pre-heating on the foaming properties of skimmed milk

Cited by 51 publications

References 34 publications

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

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

Functional properties of milk proteins as affected by enzymatic oligomerisation

Electrostatic complexes of whey protein and pectin as foaming and emulsifying agents

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