Comparative study on foaming and emulsifying properties of different beta-lactoglobulin aggregates

Hu, Jing; Yang, Jixin; Xu, Yao; Zhang, Ke; Nishinari, Katsuyoshi; Phillips, Glyn O.; Fang, Yapeng

doi:10.1039/c9fo00940j

Cited by 33 publications

(19 citation statements)

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“…The complexity and high sensitivity of globular proteins to environmental conditions make it difficult to describe their impact on the mechanisms of foam (de)stabilization [8,9,11,12,14,26]. Moreover, protein aggregation (reversible or irreversible) can have complex (enhancing/inhibiting) influence on interfacial and foaming properties as compared to those of the respective native protein [8,19,[39][40][41][42][43][44]49,55]. The behavior of proteins at interfaces and in corresponding foam films and foams is governed by the interplay of the protein concentration and the solvent conditions (salt type and concentration, pH), and the unique effect of pH is of special interest.…”

Section: Introductionmentioning

confidence: 99%

β-Lactoglobulin Adsorption Layers at the Water/Air Surface: 4. Impact on the Stability of Foam Films and Foams

et al. 2020

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The complexity and high sensitivity of proteins to environmental factors give rise to a multitude of variables, which affect the stabilization mechanisms in protein foams. Interfacial and foaming properties of proteins have been widely studied, but the reported unique effect of pH, which can be of great interest to applications, has been investigated to a lesser extent. In this paper, we focus on the impact of pH on the stability of black foam films and corresponding foams obtained from solutions of a model globular protein—the whey β-lactoglobulin (BLG). Foam stability was analyzed utilizing three characteristic parameters (deviation time, transition time and half-lifetime) for monitoring the foam decay, while foam film stability was measured in terms of the critical disjoining pressure of film rupture. We attempt to explain correlations between the macroscopic properties of a foam system and those of its major building blocks (foam films and interfaces), and thus, to identify structure-property relationships in foam. Good correlations were found between the stabilities of black foam films and foams, while relations to the properties of adsorption layers appeared to be intricate. That is because pH-dependent interfacial properties of proteins usually exhibit an extremum around the isoelectric point (pI), but the stability of BLG foam films increases with increasing pH (3–7), which is well reflected in the foam stability. We discuss the possible reasons behind these intriguingly different behaviors on the basis of pH-induced changes in the molecular properties of BLG, which seem to be determining the mechanism of film rupture at the critical disjoining pressure.

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Section: Introductionmentioning

confidence: 99%

β-Lactoglobulin Adsorption Layers at the Water/Air Surface: 4. Impact on the Stability of Foam Films and Foams

et al. 2020

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“…Natural globular β-LG of high purity was extracted from raw milk by heating at 40°C for 1 h to remove lipids, precipitating casein at pH 4.6, precipitating α-albumin at pH 3.7, dialyzing against water at 4°C for 72 h, and freeze-drying (Aschaffenburg and Drewry, 1957;Hu et al, 2019). κ-Carrageenan was supplied by FMC BioPolymer (Gelcarin GP-911NF, Philadelphia, PA) and was converted into sodium type using ion exchange resin (Amberlite IR-120, Sigma Chemical Co., St. Louis, MO; Cao et al, 2015).…”

Section: Methodsmentioning

confidence: 99%

“…In previous works, an intramolecular soluble proteinpolysaccharide complex was found to efficiently stabilize emulsions and protect PUFA (Li et al, 2012a(Li et al, , 2013Yao et al, 2016). In a previous study, we systematically compared the air-water and oil-water interfacial properties of NGBLG, BLGF, and BLGNP, and found that their foaming and emulsifying properties were in the order of BLGF > NGBLG > BLGNP (Hu et al, 2019). In this work, we prepared NGBLG, BLGNP, and BLGF and complexed each with the polysaccharide κ-carrageenan (κ-car).…”

Section: Introductionmentioning

confidence: 96%

“…Like other Pickering stabilizers, BLG aggregates can stabilize foams and emulsions via irreversible adsorption to the interface (Dickinson, 2012;Lam et al, 2014). β-Lactoglobulin fibrils with well-characterized structures are reported to be effective in the stabilization of emulsion and foam (Jung et al, 2010;Serfert et al, 2014;Gao et al, 2017;Peng et al, 2017;, whereas the interfacial stabilization effect of pure BLGNP is not as successful as that of BLGF (Nicolai and Durand, 2013;Hu et al, 2019). Interfacial stabilization by BLGF is explained by the high storage modulus at the oil-water or air-water interface due to formation of the fibril network (Jung et al, 2010;Gao et al, 2017;Hu et al, 2019).…”

Section: Introductionmentioning

confidence: 99%

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Electrostatic complexation of β-lactoglobulin aggregates with κ-carrageenan and the resulting emulsifying and foaming properties

Zhao

Zhang

et al. 2020

Journal of Dairy Science

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The electrostatic complexation of protein and polysaccharide and the functional properties of the complexes are significantly affected by the structure of protein aggregates and are important in the development of new food ingredients. In this work, natural globular β-lactoglobulin (NGBLG), β-lactoglobulin nanoparticles (BLGNP), and β-lactoglobulin fibrils (BLGF) were prepared and complexed with κ-carrageenan (κ-car). Phase diagrams of the NGBLG-, BLGNP-, and BLGF-κ-car systems were established and divided into 4 regions: mixed soluble polymers (I), intramolecular soluble complex (II), intermolecular soluble complex (III), and intermolecular insoluble complex (IV). Aggregation shifted the boundaries of regions III and IV of BLGF-or BLGNP-κ-car to lower pH and higher protein aggregates/κ-car weight ratio (r), especially for BLGF-κ-car. The emulsifying and foaming properties of the 3 mixed systems were investigated in regions I and II. Complexes in region II had significantly better emulsifying properties than the corresponding mixtures in region I and the pure protein aggregates. Interestingly, phase separation resulted in different effects on the foaming properties of the 3 BLG-κ-car complexes, in which BLGF-κ-car complexation in region II decreased the foaming properties in region I but the complexation of NGBLG-κ-car and BLGNP-κ-car in region II increased the foaming properties. The BLGF-κ-car complex in regions I and II provided the best emulsifying and foaming properties. Interfacial data both on oil-water and air-water interfaces overall explained the emulsifying and foaming properties of the complexes.

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“…Globular proteins, such as whey, pea or soy proteins, are typically objects of a few nm diameter. Upon heating, they denature and aggregate into a large range of structures, which can be imaged by simple deposition onto freshly cleaved mica and AFM observation in air or in liquid (Demanèche, Chapel, Monrozier, & Quiquampoix, 2009;Farrokhi, Badii, Ehsani, & Hashemi, 2019;Hu et al, 2019;Ikeda & Morris, 2002;Liu & Wang, 2011;Touhami & Dutcher, 2009;Wei, Cheng, & Huang, 2019;Wei & Huang, 2020). In binary mixtures, single aggregated units may even be recognized (Adal et al, 2017).…”

Section: Imaging Structures and Dynamics At Surfacesmentioning

confidence: 99%

Atomic force microscopy of food assembly: Structural and mechanical insights at the nanoscale and potential opportunities from other fields

Obeid

Guyomarc’H

2020

Food Bioscience

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Comparative study on foaming and emulsifying properties of different beta-lactoglobulin aggregates

Abstract: Different beta-lactoglobulin aggregates have different foaming and emulsifying properties.

Cited by 33 publications

References 51 publications

β-Lactoglobulin Adsorption Layers at the Water/Air Surface: 4. Impact on the Stability of Foam Films and Foams

β-Lactoglobulin Adsorption Layers at the Water/Air Surface: 4. Impact on the Stability of Foam Films and Foams

Electrostatic complexation of β-lactoglobulin aggregates with κ-carrageenan and the resulting emulsifying and foaming properties

Atomic force microscopy of food assembly: Structural and mechanical insights at the nanoscale and potential opportunities from other fields

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