The influence of temperature on the foaming of milk

Kamath, S.; Huppertz, Thom; Houlihan, Avis; Deeth, Hilton C.

doi:10.1016/j.idairyj.2008.05.001

Cited by 63 publications

(58 citation statements)

References 23 publications

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“…It had been reported that foams produced by heat‐treated protein (above 80 °C) had smaller bubble size than foams prepared from unheated protein (Nicorescu and others ). Higher viscosity of continuous phase led to smaller average bubble size (Kamath and others ; Borcherding and others ). Yang and Foegeding () found linear relationships between initial bubble size and foam stability for egg white protein and whey protein.…”

Section: Resultsmentioning

confidence: 97%

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: Resultsmentioning

confidence: 97%

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

Wang

Zhang

Vardhanabhuti

2015

Journal of Food Science

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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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“…Most effective cold aeration processes are achieved when the air is sparged into the milk through a nozzle or other type of perforated surface, e.g. sintered glass, to create small air bubbles, which are rapidly stabilised by the surface‐active materials in milk (Kinsella 1981; Walstra 2003; Kamath et al. 2008a).…”

Section: Formation Stability and Evaluation Of Milk Foamsmentioning

confidence: 99%

“…10–15 min, is often required. Changes in the appearance of a skim milk foam as a function of storage time following foaming are reported by Kamath et al. (2008a) and Borcherding et al.…”

Section: Formation Stability and Evaluation Of Milk Foamsmentioning

confidence: 99%

Foaming properties of milk: A review of the influence of composition and processing

Huppertz¹

2010

Int J of Dairy Tech

Self Cite

113

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Milk foams can be either desirable, e.g. for cappuccino-style beverages, or undesirable, e.g. in the reconstitution of milk powders or infant formula. In this article, compositional and processing factors affecting the foaming properties of milk are reviewed. Skim milk foams can be extremely stable, particularly when they are formed at 40-50°C. The presence of lipids can be detrimental to the formation and stability of milk foams, particularly at a temperature where the milk fat is partially crystalline, e.g. 20°C. The presence of phospholipids, free fatty acids and partial glycerides strongly impairs foaming of milk.

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The influence of temperature on the foaming of milk

Cited by 63 publications

References 23 publications

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

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

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

Foaming properties of milk: A review of the influence of composition and processing

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