Heteroprotein complex coacervation: A generic process

T Croguennec, GM Tavares, S Bouhallab - Advances in Colloid and …, 2017 - Elsevier
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 …

Heteroprotein complex coacervation: Focus on experimental strategies to investigate structure formation as a function of intrinsic and external physicochemical …

J Zheng, C Tang, W Sun - Advances in Colloid and Interface Science, 2020 - Elsevier
Proteins are important components of foods, because they are one of the essential food
groups, they have many functional properties that are very useful for modifying the …

Coupling and decoupling of rotational and translational diffusion of proteins under crowding conditions

M Roos, M Ott, M Hofmann, S Link… - Journal of the …, 2016 - ACS Publications
Molecular motion of biopolymers in vivo is known to be strongly influenced by the high
concentration of organic matter inside cells, usually referred to as crowding conditions. To …

Heteroprotein complex coacervation: Bovine β-lactoglobulin and lactoferrin

Y Yan, E Kizilay, D Seeman, S Flanagan, PL Dubin… - Langmuir, 2013 - ACS Publications
Lactoferrin (LF) and β-lactoglobulin (BLG), strongly basic and weakly acidic bovine milk
proteins, form optically clear coacervates under highly limited conditions of pH, ionic …

Structure and morphology of bovine serum albumin–lysozyme (BSA–Lys) complex films at air–water interface

RJ Sarmah, S Kundu - Food Hydrocolloids, 2022 - Elsevier
The heteroprotein complex formed between the two globular proteins, bovine serum
albumin and lysozyme was studied at the air–water interface by varying the subphase pH …

Soft-matter approaches for controlling food protein interactions and assembly

A Boire, D Renard, A Bouchoux… - Annual review of …, 2019 - annualreviews.org
Animal-and plant-based proteins are present in a wide variety of raw and processed foods.
They play an important role in determining the final structure of food matrices. Food proteins …

Coacervates and coaggregates: Liquid–liquid and liquid–solid phase transitions by native and unfolded protein complexes

K Iwashita, A Handa, K Shiraki - International journal of biological …, 2018 - Elsevier
Coacervates are self-assemblies formed by oppositely charged macromolecules in aqueous
solution. Although coacervates usually take a homogeneous spherical shape with …

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

GM Tavares, T Croguennec, P Hamon, AF Carvalho… - Food …, 2015 - Elsevier
This work reports on the impact of subtle change of protein charge on coacervation and
subsequent liquid–liquid phase separation between two oppositely charged globular …

Anisotropic interactions in protein mixtures: self assembly and phase behavior in aqueous solution

A Kurut, BA Persson, T Åkesson… - The Journal of …, 2012 - ACS Publications
Recent experimental studies show that oppositely charged proteins can self-assemble to
form seemingly stable microspheres in aqueous salt solutions. We here use parallel …

Spontaneous assembly and induced aggregation of food proteins

S Bouhallab, T Croguennec - … Complexes in the Dispersed and Solid State …, 2014 - Springer
Beyond their nutritional value, food proteins are a versatile group of biopolymers with a
considerable number of functionalities throughout their extensive structures, conformations …