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.

Mixed dairy and plant-based yogurt alternatives: Improving their physical and sensorial properties through formulation and lactic acid bacteria cocultures.

Food transition requires incorporating more plant-based ingredients in our diet, thus leading to the development of new plant-based products, such as yogurt alternatives (YAs). This study aimed at evaluating the impact of lactic acid bacteria (LAB) cocultures and formulation on the physico-chemical and sensory properties of YAs. YAs were made by emulsifying anhydrous milk fat (AMF) or coconut oil in milk and lupin protein suspensions.

Aroma-retention capacities of functional whey protein aggregates: Study of a strawberry aroma in solutions and in fat-free yogurts.

The aroma-retention capacity of functional whey protein aggregates (WPA) was compared to that of native whey protein isolate (WPI) in aqueous solutions and in fat-free yogurts. The retention of aroma compounds, constituting a model strawberry aroma, was evaluated by calculating gas-matrix partition coefficients using headspace gas chromatography (HS-GC). The retention capacity of WPA differed from the one of WPI for three out of seven aroma compounds detected in HS-GC.

Major Role of Voluminosity in the Compressibility and Sol-Gel Transition of Casein Micelle Dispersions Concentrated at 7 °C and 20 °C.

The objective of this work is to bring new information about the influence of temperatures (7 °C and 20 °C) on the equation of state and sol-gel transition behavior of casein micelle dispersions. Casein micelle dispersions have been concentrated and equilibrated at different osmotic pressures using equilibrium dialysis at 7 °C and 20 °C. The osmotic stress technique measured the osmotic pressures of the dispersions over a wide range of concentrations.

The surface properties of milk fat globules govern their interactions with the caseins: Role of homogenization and pH probed by AFM force spectroscopy.

The surface of milk fat globules consists of a biological membrane rich in polar lipids and glycoproteins. However, high shear stress applied upon homogenization disrupts the membrane and leads to the adsorption of casein micelles, as the major protein fraction of milk. These changes in the interface properties could affect the interactions between native or homogenized milk fat globules and the surrounding protein matrix, at neutral pH and upon acidification.

Influence of casein on the formation of whey protein microparticles obtained by dry heating at an alkaline pH.

Dry heating (DH) at 100 °C for 36 h of a whey protein isolate powder conditioned at pH 9.5 leads to the formation of stable, large and porous whey protein microparticles (PMs), resulting from the crosslinking of proteins inside the powder. These PMs could be used as high-viscosity food ingredients.

Dry heating of whey proteins leads to formation of microspheres with useful functional properties.

Modification of whey protein isolate (WPI) powders is used in the food industry to enhance the functional properties of WPI. We investigated the impact of severe dry heating (DH) at 100 °C for up to 36 h on an alkaline-treated (pH 9.5), spray dried (water activity of ~0.

Dry heating of whey proteins.

Whey protein products are of widespread use as food ingredients because of their high nutritional, biological and functional properties. Whey proteins are important structural components in many foods as used in their native form, for example for their heat-induced gelation abilities. Furthermore, they also offer reliable functionalities when modified by heating processes as denatured or aggregated proteins.

Lipid droplets coated with milk fat globule membrane fragments: Microstructure and functional properties as a function of pH.

Processed lipid droplets coated by milk fat globule membrane (MFGM) material are of primary interest to mimic the specific functions provided by the fat globules in milk and dairy products. The objectives were to investigate, as a function of pH, the properties and microstructure of MFGM-coated lipid droplets prepared with an ingredient rich in MFGM containing polar lipids and proteins. The samples were prepared in water and in milk ultrafiltrate.

Immunomodulation properties of multi-species fermented milks.

Dairy propionibacteria (PAB) are used as a ripening starter in combination with Lactic acid bacteria (LAB) for dairy products such as Swiss-type cheese. LAB and PAB have also been studied for their probiotic properties but little is still known about their individual and/or synergistic beneficial effects within dairy matrices. In the context of a rising incidence of Inflammatory Bowel Diseases, it has become crucial to evaluate the immunomodulatory potential of bacteria ingested in large numbers via dairy products.

Casein Compared with Whey Proteins Affects the Organization of Dietary Fat during Digestion and Attenuates the Postprandial Triglyceride Response to a Mixed High-Fat Meal in Healthy, Overweight Men.

Background: Postprandial lipemia is a risk factor for cardiovascular disease. The potential impacts of the type/nature of dietary protein on postprandial lipemia and associated dysregulations have been insufficiently investigated.

Objective: We investigated the postprandial effect of including in a high-fat meal some milk protein fractions that markedly differ in their physicochemical properties and composition [either casein (CAS), whey protein (WHE), or α-lactalbumin-enriched whey protein (LAC)].

The heat treatment and the gelation are strong determinants of the kinetics of milk proteins digestion and of the peripheral availability of amino acids.

This study aimed to determine the kinetics of milk protein digestion and amino acid absorption after ingestion of four dairy matrices by six minipigs: unheated or heated skim milk and corresponding rennet gels. Digestive contents and plasma samples were collected over a 7 h-period after meal ingestion. Gelation of milk slowed down the outflow of the meal from the stomach and the subsequent absorption of amino acids, and decreased their bioavailability in peripheral blood.

Nisin quantification by ELISA allows the modeling of its apparent diffusion coefficient in model cheeses.

The diffusion of small solutes in cheese is of key importance for most enzymatic reactions involved in the ripening process. However, only a limited amount of data is available on salt diffusion and practically none on peptide diffusion. Nisin, a bacteriocin peptide, migrated in model cheeses made from ultrafiltered (UF) retentate.

Characterization of heat-induced changes in skim milk using asymmetrical flow field-flow fractionation coupled with multiangle laser light scattering.

Separation and size measurement of protein particles are a relevant approach to monitor heat-induced changes in skim milk. Unfortunately, no method is currently available at low cost and without excessive preparation of the samples. Therefore, the present study aimed at evaluating the interest of asymmetrical flow field-flow fractionation (AFlFFF) coupled with multiangle laser light scattering (MALLS) for this purpose.

Role of the heat-induced whey protein/kappa-casein complexes in the formation of acid milk gels: a kinetic study using rheology and confocal microscopy.

The effect of heat treatment of milk on the formation of acid gel was examined using confocal scanning laser microscopy and low-amplitude dynamic oscillation throughout acidification. Milk samples were reconstituted by mixing colloidal phase from unheated or preheated skim milk, labeled with rhodamine B isothiocyanate, with the aqueous phase from unheated or preheated milk, labeled with fluorescein isothiocyanate. Gels were made by acidification with glucono-delta-lactone.

Acid gelation properties of heated skim milk as a result of enzymatically induced changes in the micelle/serum distribution of the whey protein/kappa-casein aggregates.

Changes in the acid gelation properties of skim milk as a result of variations in the micelle/serum distribution of the heat-induced whey protein/kappa-casein aggregates, induced by the combination of heat treatment and limited renneting, were investigated. No dramatic change in the zeta potential or the isoelectric point of the casein micelles was suggested, whether the aggregates were all attached to the casein micelle or not. Fluorescence intensity measurement using 8-anilino-1-naphthalenesulfonic acid (ANS) showed that the heat-induced aggregates were highly hydrophobic.

Determination of exposed sulfhydryl groups in heated beta-lactoglobulin A using IAEDANS and mass spectrometry.

This paper takes a new approach to determining which sulfhydryl groups are exposed during the heat denaturation of bovine beta-lactoglobulin A. The sulfhydryl groups exposed after heating were blocked with 5-((((2-iodoacetyl)amino)ethyl)amino)naphthalene-1-sulfonic acid (IAEDANS). The results show that IAEDANS is a suitable blocking agent, and its absorbance at 336 nm enabled the quantification of exposed sulfhydryl groups in a mixture of protein species by gel permeation chromatography.

pH-Dependent behaviour of soluble protein aggregates formed during heat-treatment of milk at pH 6.5 or 7.2.

The pH-dependent behaviour of soluble protein aggregates produced by the pre-heating of reconstituted skim milk at 90 degrees C for 10 min was studied, in order to understand the role of these aggregates in acid gelation of heated milk. The following milk samples were prepared: (1) control (unheated reconstituted milk, pH 6.5); (2) milk heat-treated at pH 6.