Selective coacervation between lactoferrin and the two isoforms of β-lactoglobulin

Tavares, Guilherme M.; Croguennec, Thomas; Hamon, Pascaline; Carvalho, Antônio Fernandes de; Bouhallab, Saı̈d

doi:10.1016/j.foodhyd.2015.02.027

Cited by 49 publications

(48 citation statements)

References 31 publications

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“…However, for Yan et al [57], coacervates were formed at protein concentration between 10 g L -1 and 40 g L -1 at the optimal protein mixing ratio. Below 10 g L -1 , β-LG and LF mixture does not lead to coacervate in agreement with Tavares et al [61]. The disappearance of the coacervates at high protein concentration was linked to the self-aggregation of β-LG leading to a progressive depletion of free β-LG [57].…”

Section: Effect Of Protein Concentrationsupporting

confidence: 89%

“…The LF/β-LG complex coacervation was found to be highly sensitive to ionic strength and occurs for values below 25 mM [57,61]. However, other results showed the occurrence of such coacervation at ionic strength as high as 100 mM [58].…”

Section: Effect Of Ionic Strengthmentioning

confidence: 92%

“…The differences in the pH range for LF/β-LG coacervation reported by Yan et al [57] and Anema and de Kruif [58] could be explained by i-different protein concentrations investigated and consequently different buffering capacity of the system modulating pH drift, ii-and/or certain specificity linked to the β-LG variant used. Working in buffer to prevent any protein association induced pH drift, Tavares et al [61] observed that LF/β-LG coacervates were formed in the pH range 5.5 -6.0 using a mixture of variant A and B of β-LG. On both side of this pH range, particles assigned to LF/β-LG aggregates were…”

Section: Accepted Manuscriptmentioning

confidence: 99%

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Heteroprotein complex coacervation: A generic process

Croguennec

Tavares

Bouhallab

2017

Advances in Colloid and Interface Science

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Proteins exhibit a rich diversity of functional, physico-chemical and biodegradable properties which makes them appealing for various applications in the food and non-food sectors. Such properties are attributed to their ability to interact and assemble into a diversity of supramolecular structures. The present review addresses the updated research progress in the recent field of complex coacervation made from mixtures of oppositely charged proteins (i.e. heteroprotein systems). First, we describe briefly the main proteins used for heteroprotein coacervation. Then, through some selected examples, we illustrate the particularity and specificity of each heteroprotein system and the requirements that drive optimal assembly into coacervates. Finally, possible and promising applications of heteroprotein coacervates are mentioned.

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Section: Effect Of Protein Concentrationsupporting

confidence: 89%

Section: Effect Of Ionic Strengthmentioning

confidence: 92%

Section: Accepted Manuscriptmentioning

confidence: 99%

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Heteroprotein complex coacervation: A generic process

Croguennec

Tavares

Bouhallab

2017

Advances in Colloid and Interface Science

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“…The self-assembly of these materials is driven by entropy, where the initial electrostatic attraction between oppositely-charged macro-ions results in the release of small, bound counter-ions and the restructuring of water molecules [1][2][3][4]. Complex coacervates have a long history of use in the food [5][6][7][8][9][10][11][12][13] and personal care [14,15] industries, and have found increasing utility as a platform for drug and gene delivery [1][2][3][4], as well as underwater adhesives [5][6][7][8][9][10][11][12][13][48][49][50][51][52][53][54][55][56][57][58][59][60][61][62]. Coacervation has also recently been implicated in the formation of various biological assemblies [1,[14][15][16]55,…”

Section: Introductionmentioning

confidence: 99%

Linear viscoelasticity of complex coacervates

Liu

Winter

Perry

2017

Advances in Colloid and Interface Science

129

163

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Rheology is a powerful method for materials characterization that can provide detailed information about the self-assembly, structure, and intermolecular interactions present in a material. Here, we review the use of linear viscoelastic measurements for the rheological characterization of complex coacervate-based materials. Complex coacervation is an electrostatically and entropically-driven associative liquid-liquid phase separation phenomenon that can result in the formation of bulk liquid phases, or the self-assembly of hierarchical, microphase separated materials. We discuss the need to link thermodynamic studies of coacervation phase behavior with characterization of material dynamics, and provide parallel examples of how parameters such as charge stoichiometry, ionic strength, and polymer chain length impact self-assembly and material dynamics. We conclude by highlighting key areas of need in the field, and specifically call for the development of a mechanistic understanding of how molecular-level interactions in complex coacervate-based materials affect both selfassembly and material dynamics.

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“…In this case, ITC revealed an exothermic interaction with contributions from both enthalpy and entropy contributions. The study also reported that the interaction involved at least two steps requiring two independent binding sites (TAVARES et al, 2015).…”

Section: Isothermal Titration Calorimetry (Itc)mentioning

confidence: 92%