Implications of interfacial characteristics of food foaming agents in foam formulations

Patino, Juan M. Rodrı́guez; Sánchez, Cecilio Carrera; Niño, Ma. Rosario Rodríguez

doi:10.1016/j.cis.2007.12.007

Cited by 186 publications

(88 citation statements)

References 177 publications

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“…The results show that heat had diverse effects on interfacial behaviors of soy protein products, which might have been due to structural and/or conformational changes (Rodríguez Patino et al . ; Ruíz‐Henestrosa et al . ).…”

Section: Resultsmentioning

confidence: 99%

Modification of Foaming Properties of Commercial Soy Protein Isolates and Concentrates by Heat Treatments

Shao

Lin

Kao

2016

Journal of Food Quality

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Commercial soy protein isolates (SPIs; China 980A, China 880, ISP 974 and ADM 974) and soy protein concentrates (SPCs; SPC 700 and ARCON S) were used for comparing the effects of heat treatment (55C and 85C for 10–30 min) on the surface tension, surface hydrophobicity, viscosity, solubility at pH 3–8 and foaming properties. The foam capacity was highly positively correlated with the surface hydrophobicity, but negatively related to the surface tension, liquid percentage and foam maximum density. Heating commercial SPIs and SPCs improved the foam capacity, changed the surface hydrophobicity, solubility, foam maximum density and foam stability, and decreased the surface tension and viscosity. The heating temperatures had a greater influence on protein properties than did the heating time. Among soy protein products, heat‐modified China 980A had the best foam capacity and foam stability. Practical Applications Simple heating treatments improved foaming properties of commercial soy products with low level of surface tension and high level of surface hydrophobicity and solubility. In particular, heating improved surface tension, foaming capacity, liquid percentage, foam maximum density and not damaged foaming stability in most of samples. These results indicate that a relatively inexpensive, high quality foaming properties was obtained by the action of heating process that benefits the application of using commercial soy proteins as foaming agents in aerated food systems. Therefore, the foaming properties of heated soy proteins were dramatically different, showing great potential for improving tailor‐made proteins for various applications.

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Section: Resultsmentioning

confidence: 99%

Modification of Foaming Properties of Commercial Soy Protein Isolates and Concentrates by Heat Treatments

Shao

Lin

Kao

2016

Journal of Food Quality

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“…Proteins and peptides play a major role in forming and stabilising foams in aerated food products. Factors like heat treatment, pH and ionic environment have a significant influence on the foaming properties of milk proteins, as reported in detail by a number of authors (Campbell & Mougeot, 1999;Davis & Foegeding, 2007;Murray, 2007;Rodriguez Patino, Carrera Sanchez, & Rodriguez Nino, 2008;Rullier, Novales, & Axelos, 2008;Zhang, Dalgleish, & Goff, 2004).…”

Section: Introductionmentioning

confidence: 89%

Influence of glycosylation on foaming properties of bovine caseinomacropeptide

Kreuß

Krause

Kulozik

2009

International Dairy Journal

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“…The dissociation degree of ionized groups of proteins depends on the pH of the solution. In acidic media, the dissociation of carboxylic groups is suppressed and poly-ions mainly contain positively charged -RNH 3 + groups. The dissociation degree of amino groups increases in slightly acidic media.…”

Section: Effect Of Ph On the Stability Of Foammentioning

confidence: 99%

“…The initial solution of the surfactant in the amount of 10 cm 3 was pipetted into a cylinder with a capacity of 50-100 cm 3 . The cylinder was shaken for 20 s. After shaking, a stopwatch was switched on, simultaneously marking the volume of the cylinder content (V) and the volume of the remaining liquid (V r ).…”

Section: Methodsmentioning

confidence: 99%

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Composite Foaming Agents on the Basis of High-Molecular Natural Surfactants

Amankeldi

Ospanova

Мusabekov

2018

Colloids and Interfaces

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Today, naturally occurring foam constituents and surface-active proteins with intriguing structures and functions are being identified from a variety of biological and chemical sources. In this paper we studied the colloid chemical properties of high-molecular natural surfactants such as keratin hydrolyzate (1.5-15%), gelatin (0.1-1%), and egg albumin (0.1-1%) in a wide concentration range. The foaming ability and foam-stabilizing properties of mixtures of these proteins were established. The high stability of foams obtained from mixtures of surfactants can be explained by the formation of mixed structured layers from the surface-active associates, promoting the thickening of foam films. The ratio of polymer mixtures was optimized (keratin (15%)-albumin (1%) (1:1)) to produce high-quality foaming agents. The foam parameters such as surface tension, capillary pressure of the Plateau-Gibbs channels, radii of curvature, critical micelle concentration, and relative viscosity were defined. The high surface activity and foam stability corresponds to a pH close to the isoelectric state of the proteins. This occurs due to the conformational changes of macromolecules of the protein at the liquid-gas interface, forming particles of colloidal size.

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Implications of interfacial characteristics of food foaming agents in foam formulations

Cited by 186 publications

References 177 publications

Modification of Foaming Properties of Commercial Soy Protein Isolates and Concentrates by Heat Treatments

Modification of Foaming Properties of Commercial Soy Protein Isolates and Concentrates by Heat Treatments

Influence of glycosylation on foaming properties of bovine caseinomacropeptide

Composite Foaming Agents on the Basis of High-Molecular Natural Surfactants

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