Protein aggregation induced by phase separation in a pea proteins–sodium alginate–water ternary system

Mession, Jean-Luc; Assifaoui, Ali; Lafarge, Céline; Saurel, Rémi; Cayot, Philippe

doi:10.1016/j.foodhyd.2011.12.022

Cited by 40 publications

(35 citation statements)

References 35 publications

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“…98 In a pea protein isolate-sodium alginate-water tertiary mixture, flow behavior depends on biopolymer concentration and, further, viscosity of sodium alginate has a high influence. 30 Increase in viscosity was reported in soybean isolate and xanthan gum emulsions by Xie and Hettiarachchy. 91 When protein and polysaccharides are in a complex network with weak electrostatic interactions and hydrogen bonding, they hold a large amount of water.…”

Section: Viscositymentioning

confidence: 86%

“…Further, structural rearrangements upon shearing also need to be considered to determine the viscoelastic behavior of the protein–polysaccharide system in addition to the effect of molecular weight of polysaccharides, pH, ionic strength and temperature . In a pea protein isolate–sodium alginate–water tertiary mixture, flow behavior depends on biopolymer concentration and, further, viscosity of sodium alginate has a high influence . Increase in viscosity was reported in soybean isolate and xanthan gum emulsions by Xie and Hettiarachchy …”

Section: Functional Properties Of Protein–polysaccharide Complexesmentioning

confidence: 99%

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Review on plant protein–polysaccharide complex coacervation, and the functionality and applicability of formed complexes

2018

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Controlling the interactions between plant proteins and polysaccharides can lead to the development of novel electrostatic complexed structures that can give unique functionality. This in turn can broaden the diversity of applications that they may be suitable for. Overwhelmingly in the literature, work and reviews relating to coacervation have involved the use of animal proteins. However, with the increasing demand for plant-based protein alternatives by industry and consumers, a greater understanding of how they interact with polysaccharides is essential to control structure, functionality and applicability. This review discusses the factors governing the nature of protein-polysaccharide interactions, their functional attributes and industrial applications, with special attention given to plant proteins. © 2018 Society of Chemical Industry.

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Section: Viscositymentioning

confidence: 86%

Section: Functional Properties Of Protein–polysaccharide Complexesmentioning

confidence: 99%

Review on plant protein–polysaccharide complex coacervation, and the functionality and applicability of formed complexes

2018

View full text Add to dashboard Cite

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“…Proteins from different sources differ in their amino acid sequence, tertiary structures, molar mass, and distribution of reactive groups. All of these features can contribute to different functionalities in different environmental conditions when these proteins interact with polysaccharides (Andrade et al, 2010;Elmer et al, 2011;Mession et al, 2012;Miquelim et al, 2010;Souza et al, 2013;Tran & Rousseau, 2013;Yin et al, 2012).…”

Section: Discussionmentioning

confidence: 99%

Milk Protein–Polysaccharide Interactions

2014

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“…This neutral polysaccharide from the group of mannans is well-known by its thickening capacity. There are several studies about protein-polysaccharide interactions in aqueous solution (de Kruif & Tuinier, 2001;Turgeon et al, 2003;Schaink & Smit, 2007;Mession et al, 2012), and some of them evaluated the interaction between these ingredients in cold-set gels (Valim et al, 2008;de Jong et al, 2009;Vilela et al, 2011). However, to our knowledge, there are no studies about acid gels composed by soy protein isolate and LBG.…”

Section: Introductionmentioning

confidence: 99%

Acid gelation of native and heat‐denatured soy proteins and locust bean gum

Perrechil

Braga

Cunha

2012

Int J of Food Sci Tech

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Summary The effects of protein concentration and locust bean gum (LBG) addition on the mechanical properties, microstructure and water holding capacity of acidified soy protein (SPI) gels were studied. The protein was employed in two different states: (i) native and (ii) heat denatured. A slow acidification rate was induced in both systems by applying glucono‐δ‐lactone (GDL). The results indicated that the gels of native SPI were weaker, less deformable and showed lower water holding capacity than the gels of heat‐denatured SPI. The LBG addition led to an increase in the strength and water holding capacity of SPI gels, independent of the protein state (native or denatured). These results indicated that the properties of texture and water holding capacity of the SPI acid gels can be modulated by the process conditions or by the addition of other ingredients, such as polysaccharides.

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Protein aggregation induced by phase separation in a pea proteins–sodium alginate–water ternary system

Cited by 40 publications

References 35 publications

Review on plant protein–polysaccharide complex coacervation, and the functionality and applicability of formed complexes

Review on plant protein–polysaccharide complex coacervation, and the functionality and applicability of formed complexes

Milk Protein–Polysaccharide Interactions

Acid gelation of native and heat‐denatured soy proteins and locust bean gum

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