Viscoelastic and flow behaviour of β-lactoglobulin/lactoferrin coacervates: Influence of temperature and ionic strength.

Heteroprotein complex coacervation has potential for a wide range of applications. However, the sensitivity of coacervates to slight changes in physico-chemical conditions may constitute a technological barrier for their development and deserves to be better understood. In this study, the rheological properties of β-lactoglobulin/lactoferrin (βLG/LF) heteroprotein complex coacervates were investigated with respect to narrow changes of temperature (5-40 °C) and ionic strength (0 to 10 mM added NaCl).

Component Distribution, Shear-Flow Behavior, and Sol-Gel Transition in Mixed Dispersions of Casein Micelles and Serum Proteins.

The shear flow and solid-liquid transition of mixed milk protein dispersions with varying concentrations of casein micelles (CMs) and serum proteins (SPs) are integral to key dairy processing operations, including microfiltration, ultrafiltration, diafiltration, and concentration-evaporation. However, the rheological behavior of these dispersions has not been sufficiently studied. In the present work, dispersions of CMs and SPs with total protein weight fractions () of 0.

Non-linear properties and yielding of enzymatic milk gels.

One of the first steps of cheese making is to suppress the colloidal stability of casein micelles by enzymatic hydrolysis and initiate milk gelation. Afterwards, the enzymatic milk gel is cut to promote syneresis and expulsion of the soluble phase of milk. Many studies have reported on the rheological properties of enzymatic milk gels at small strain, but they provide limited information on the ability of the gel to be cut and handled.

Ionic Strength Dependence of the Complex Coacervation between Lactoferrin and β-Lactoglobulin.

Heteroprotein complex coacervation is an assembly formed by oppositely charged proteins in aqueous solution that leads to liquid-liquid phase separation. The ability of lactoferrin and β-lactoglobulin to form complex coacervates at pH 5.5 under optimal protein stoichiometry has been studied in a previous work.

Heat treatment of milk protein concentrates affects enzymatic coagulation properties.

Dairy ingredients with highly concentrated protein contents are high added value products with expanding market. The manufacture of such ingredients includes a succession of unit operations of which heat treatment is a key step to guarantee the microbial safety, that induces major changes in protein structures and thus ingredients functionalities. However, due to an incomplete understanding of phenomena taking place at high protein concentrations, shedding light on their mechanisms is a scientific challenge as well as an industrial need.