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The purpose of this study was to improve understanding of the structural and functional property changes that milk-protein concentrates undergo during production, particularly how the manufacturing route (heat treatment position and intensity), standardization (in osmosed water or ultrafiltrate permeate) and formulation (casein:whey protein (Cas:WP) ratio) influence the physico-chemical characteristics-hygroscopicity, particle size, sphericity, density and evolution of browning during storage. To obtain a comprehensive understanding of the parameters responsible for the distinctive characteristics of different powders, a multifactorial approach was adopted. Hygroscopicity depended mainly on the standardizing solution and to a lesser extent the Cas:WP ratio. The particle size of the heat-treated casein-dominant powders was up to 5 μm higher than for those that had had no heat treatment regardless of the standardizing solution, which also had no influence on the sphericity of the powder particles. The density of the powders increased up to 800 kg·m -3 with a reduced proportion of casein, and lactose and whey proteins participated in browning reactions during storage at 13 °C. In increasing order, the modality of heat treatment, the standardizing solution and the Cas:WP protein ratio influenced the key characteristics. This work is relevant for industrial applications to increase control over the functionalities of powdered products.

Dairy powders are mainly produced by droplet spray drying, an articulated process that enables the manufacture of high added-value goods with a long shelf life and well-preserved functional properties. Despite the recent advances, a full understanding of the mechanisms occurring at the droplet scale in drying towers and, consequently, of the impact of process parameters and processed fluid characteristics on the powder properties is far from being achieved. In the wake of previous studies based on a laboratory scale approach, in this work, we provided a global picture of the drying in droplets of dairy protein mixes, i.e., whey proteins and casein micelles, which represent crucial dairy powder ingredients. Using profile visualization and optical microscopy, we explored the shape evolution in droplets with a range of protein contents and compositions typical of commercial powder production. The observation favored the evaluation of the specific role of each protein on the evaporation dynamics, and led to the construction of a phase diagram predictive of the dry droplet shape starting from the characteristics of the initial protein dispersions. Our outcomes represent a further step shedding light on the paradigm linking the physics of drying at the microscale and the nutritional properties of complex dairy powders.

Hypothesis: The effective contribution of interfacial properties to the rheology of foams is a source of many open questions. Film dynamics during topological T1 changes in foams, essentially studied for low molecular weight surfactants, and scarcely for proteins, could connect interfacial properties to protein foam rheology., Experiments: We modified whey protein isolate (WPI), and its purified major protein β-lactoglobulin (β-lg) by powder pre-conditioning and dry-heating in order to obtain a broad variety of interfacial properties. We measured interfacial properties, film relaxation duration after a T1 event and bulk foam rheology., Findings: We found that, for β-lg, considered as a model protein, the higher the interfacial elastic modulus, the longer the duration of topological T1 changes and the greater the foam storage and loss moduli and the yield stress. However, in the case of the more complex WPI, these correlations were less clear. We propose that the presence in WPI of other proteins, lactose and minerals modify the impact of pre-conditioning and dry-heating on proteins and thereby, their behaviour at the interface and inside the liquid film., (Copyright © 2019 Elsevier Inc. All rights reserved.)

We have compared the behavior of ovotransferrin at the air-solution interface in the presence of a monovalent ion (acetate), or a divalent ion (citrate), the latter being known to induce conformational changes of this protein upon interaction with its iron-binding sites. We have characterised the adsorption layer at the air-water interface in terms of homogeneity, surface concentration excess and rheological properties at pH 4.0. Besides we have investigated the bulk conformation in the presence of the two anions. In the presence of citrate only, interfacial layers display well-defined domains of higher overall surface concentration suggesting multilayers adsorption. Citrate also induces higher helical content and stabilizes the protein against thermal denaturation. Hence we propose that these changes are involved in the propensity of ovotransferrin to self-assemble at the air-water interface resulting in thick and heterogeneous interfacial layer., (Copyright © 2014 Elsevier Inc. All rights reserved.)

Adsorption of purified apo-ovotransferrin at the air-water interface was studied by ellipsometry, surface tension, polarization-modulation infrared reflection-absorption spectroscopy (PM-IRRAS), and shear elastic constant measurements. No significant difference was observed between pH 6.5 and 8.0 as regards the final value of surface concentration and surface pressure. However at low concentration, a weak barrier to adsorption is evidenced at pH 6.5 and confirmed by PM-IRRAS measurements. At a pH where the protein net charge is negative (pH 8.0), the behavior of ovotransferrin at the air-water interface is more influenced by charge effects rather than bulk concentration effects. At this pH, the interface exhibits a low shear elastic constant and a spectral signature not usual for globular proteins., (Copyright © 2011 Elsevier Inc. All rights reserved.)