Stabilization of foams and emulsions by mixtures of surface active food-grade particles and proteins

• 发表在: Food Hydrocolloids
• 主要作者: 2-s2.0-79851507689
• 格式: 文件
• 语言: English
• 出版: Elsevier B.V. 2011
• 在线阅读: https://www.scopus.com/inward/record.uri?eid=2-s2.0-79851507689&doi=10.1016%2fj.foodhyd.2010.07.025&partnerID=40&md5=97a8c4a125bb574bd489d6f63c8a09d7

Surface active biopolymers such as proteins can form films with particularly high interfacial elasticities and viscosities and these molecules are widely exploited as foaming and emulsifying agents in foods. Solid particles of the correct size and wetting characteristics can also be extremely effective stabilizers of foams and emulsions, although the underlying mechanism of stabilization is somewhat different. Relatively little is known about what happens when both surface active polymers and surface active particles are present together. This work presents recent findings on the effects of mixtures of proteins plus novel food-compatible surface active particles. The proteins include caseins and whey proteins. The surface active particles prepared include cellulose. +. ethyl cellulose complexes, hydrophobically-modified starch granule particles and stable (non-spreading) protein-stabilized oil droplets. Interfacial shear rheology of adsorbed films was measured via a biconical bob apparatus and interfacial dilatational rheology was measured via a Langmuir trough type apparatus. The corresponding stability of bubbles to coalescence and disproportionation was assessed in separate experiments. Stability of oil-in-water emulsions was assessed via measurement of particle size distributions as function of time and visual assessment of the tendency to creaming and oiling off. In general, it is shown that the surface active particles on their own exhibit much lower measures of interfacial elasticity and viscosity than the proteins, but in combination with the proteins they appear to enhance the interfacial viscoelasticity considerably, with concomitant increases in bubble and emulsion droplet stability. There is little evidence of attractive interactions between the particles and the proteins, so a possible explanation of the increased stability is that the proteins increase the accumulation of particles at the interface, giving rise to increased jamming of particles at the interface. © 2010 Elsevier Ltd.