Claire Gaiani

Thermodynamic Characterization of Acacia Gum−β-Lactoglobulin Complex Coacervation

The interactions of beta-lactoglobulin (BLG) with total acacia gum (TAG) in aqueous solutions have been investigated at pH 4.2 and 25 degrees C. Isothermal titration calorimetry (ITC) has been used to determine the type and magnitude of the energies involved in the complexation process of TAG to BLG. Dynamic light scattering (DLS), electrophoretic mobility (mu(E)), turbidity measurements (tau), and optical microscopy were used as complementary methods on the titration mode to better understand the sum of complicated phenomena at the origin of thermodynamic behavior. Two different binding steps were detected. Thermodynamic parameters indicate a first exothermic step with an association constant K(a1) of (48.4 +/- 3.6) x 10(7) M(-1) that appeared to be mostly enthalpy-driven. A positive heat capacity change was obtained corresponding at the signature for electrostatic interactions. The second binding step, 45 times less affinity (K(a2) = (1.1 +/- 0.1) x 10(7) M(-1)), was largely endothermic and more entropy-driven with a negative value of heat capacity change, indicative of a hydrophobic contribution to the binding process. The population distribution of the different species in solution and their sizes were determined through DLS. Dispersion turbidity of particles markedly increased and reached a maximum at a 0.015 TAG/BLG molar ratio. Largely more numerous coacervates appeared at this molar ratio (0.015) and two different kinds of morphologies were noticed for the large coacervates. Above the TAG/BLG molar ratio of 0.015, dispersions turbidity decreased, which might be due to an excess of negative charges onto particles as revealed by electrophoretic mobility measurements. The results presented in this study should provide information about the thermodynamic mechanisms of TAG/BLG binding processes and will facilitate the application of the formed supramolecular assemblies as functional ingredients in food and nonfood systems.

Comparative study of particle structure evolution during water sorption: Skim and whole milk powders

Surface composition of dairy powders influences significantly a quantity of functional properties such as rehydration, caking, agglomeration. Nevertheless, the kinetic of water uptake by the powders was never directly related to the structure and the composition of the surface. In this work, the effect of relative humidity on the structural reorganization of two types of dairy powder was studied. The water-powder interaction for industrial whole milk powder, and skim milk powder was studied using dynamic vapor sorption. The water sorption isotherms were fitted with a Brunner-Emmet-Teller model and each stage of the sorption curve was analyzed with a Fickian diffusion. The water content in the monolayer predicted for each powder and the moisture diffusivity calculated were discussed and compared. Concurrently, powders microstructure and powders surface under variable relative humidity were assessed by X-ray photoelectron spectroscopy, scanning electron microscopy coupled with energy dispersive X-ray and atomic force microscopy. A correlation between the data obtained from the sorption isotherms and the modifications of structure allowed us to conclude that powder microstructure and chemical state of the components could play an important role in determining the water diffusivity.

In vitro interactions between probiotic bacteria and milk proteins probed by atomic force microscopy.

Interactions between microbial cells and milk proteins are important for cell location into dairy matrices. In this study, interactions between two probiotic strains, Lactobacillus rhamnosus GG and Lactobacillus rhamnosus GR-1, and milk proteins (micellar casein, native and denatured whey proteins) were studied. The bacterial surface characterization was realized with X-ray photoelectron spectroscopy (XPS) to evaluate surface composition (in terms of proteins, polysaccharides and lipid-like compounds) and electrophoretic mobility that provide information on surface charge of both bacteria and proteins along the 3-7 pH range. In addition, atomic force microscopy (AFM) enabled the identification of specific interactions between bacteria and whey proteins, in contrast to the observed nonspecific interactions with micellar casein. These specific events appeared to be more important for the GG strain than for the GR-1 strain, showing that matrix interaction is strain-specific. Furthermore, our study highlighted that in addition to the nature of the strains, many other factors influence the bacterial interaction with dairy matrix including the nature of the proteins and the pH of the media.

Lactic acid bacteria in dairy food: surface characterization and interactions with food matrix components.

This review gives an overview of the importance of interactions occurring in dairy matrices between Lactic Acid Bacteria and milk components. Dairy products are important sources of biological active compounds of particular relevance to human health. These compounds include immunoglobulins, whey proteins and peptides, polar lipids, and lactic acid bacteria including probiotics. A better understanding of interactions between bioactive components and their delivery matrix may successfully improve their transport to their target site of action. Pioneering research on probiotic lactic acid bacteria has mainly focused on their host effects. However, very little is known about their interaction with dairy ingredients. Such knowledge could contribute to designing new and more efficient dairy food, and to better understand relationships between milk constituents. The purpose of this review is first to provide an overview of the current knowledge about the biomolecules produced on bacterial surface and the composition of the dairy matter. In order to understand how bacteria interact with dairy molecules, adhesion mechanisms are subsequently reviewed with a special focus on the environmental conditions affecting bacterial adhesion. Methods dedicated to investigate the bacterial surface and to decipher interactions between bacteria and abiotic dairy components are also detailed. Finally, relevant industrial implications of these interactions are presented and discussed.

X-ray Photoelectron Spectroscopy for Wheat Powders: Measurement of Surface Chemical Composition

The functional properties of wheat powders depend largely on the surface characteristics of their particles. X-ray photoelectron spectroscopy (XPS) has been considered to investigate the surface composition of wheat powders. The objective of the present study is to evaluate the ability of XPS to discriminate wheat components and to calculate the surface composition of wheat powders. First, XPS surveys for the main wheat isolated components (starch, proteins, arabinoxylans, and lipids) were determined. XPS results demonstrate that it is able to distinguish wheat proteins, polysaccharides, and lipids, but it is not able to distinguish starch and arabinoxylan because of their similarity in chemical structure. The XPS analyses of simple reconstituted wheat flours based on two components (starch and protein) or three components (by adding arabinoxylan) demonstrated the ability of XPS to measure the surface composition of the wheat flours. The surface composition of native wheat flour demonstrated an overrepresentation of protein (54%) and lipids (44%) and an underrepresentation of starch (2%) compared to the bulk composition. Results are discussed with regard to difficulties in discriminating arabinoxylans and starch components.

Effect of dairy powders fortification on yogurt textural and sensorial properties: a review

Yogurts are important dairy products that have known a rapid market growth over the past few decades. Industrial yogurt manufacture involves different processing steps. Among them, protein fortification of the milk base is elemental. It greatly enhances yogurt nutritional and functional properties and prevents syneresis, an undesirable yogurt textural defect. Protein enrichment can be achieved by either concentration process (evaporation under vacuum and membrane processing: reverse osmosis and/or ultrafiltration) or by addition of dairy ingredients. Traditionally, skim milk powder (SMP) is used to enrich the milk base before fermentation. However, increased quality and availability of other dairy ingredients such as milk protein isolates (MPI), milk protein concentrates (MPC) whey protein isolates (WPI) and concentrates (WPC), micellar casein (MC) and caseinates have promoted their use as alternatives to SMP. Substituting different dry ingredients for skim milk powder in yogurt making affects the yogurt mix protein composition and subsequent textural and sensorial properties. This review focuses on various type of milk protein used for fortification purposes and their influence on these properties.

Characterization of high-milk-protein powders upon rehydration under various salt concentrations

Rehydration of native micellar casein and native whey isolate protein powders was followed in different ionic environments. Solutions of NaCl and CaCl2 in the concentration range of 0 to 12% (wt%) were used as rehydration media. The rehydration profiles obtained were interpreted in terms of wetting, swelling, and dispersion stages by using a turbidity method. Two behaviors were observed depending on the salt concentration. For native micellar casein powder, a significant change was observed between 3 and 6% NaCl and between 0.75 and 1.5% CaCl2. The first behavior (low salt concentration) presents a typical rehydration profile: quick wetting, swelling, and long dispersion stage. The dispersion stage of the second behavior (high salt concentration) was significantly shortened, indicating a strong modification of the protein backbone. The rehydration of whey protein powder was less influenced by salts. At low salt concentrations, a typical profile for whey powders was observed: wetting with lump formation and no swelling followed by a quick dispersion. At high CaCl2 concentrations, no turbidity stabilization was observed, indicating a possible protein unfolding and denaturation. Additionally, the changes in secondary structures of the 2 proteins upon salt increase were followed by Fourier transform infrared spectroscopy and confirmed the different profiles observed.

Combined effect of heat treatment and ionic strength on the functionality of whey proteins.

A 5% (wt/vol) whey protein isolate (WPI) dispersion (pH 6.5) with different concentrations of NaCl was submitted to dynamic heat treatment. Protein dispersions were characterized as to their rheological properties, particle sizes, morphology, denaturation temperatures, and protein surface hydrophobicity. At low ionic strength (<200 mmol/kg), gel elastic modulus increased and strongest gel stiffness was achieved. High salt concentrations lead to a weaker gel, whereas no gels at all were formed without salt. The gelation temperature was also influenced by ionic strength and an increase in denaturation temperature and thermal stability was also observed by using differential scanning calorimetry. Additionally, heat-induced changes in secondary structures upon salt augmentation were followed by Fourier transform infrared spectroscopy. Secondary structural elements estimations obtained from amide I assignments were correlated with those from amide III assignments. Upon salt increase, no differences in secondary structure were observed without heating, whereas upon heating and without salt increase, the Fourier transform infrared spectroscopy data revealed an increase in intermolecular β-sheets at the cost of β-turns and random coils, with no change in α-helical structures. However, NaCl addition along with dynamic heat treatment of WPI dispersion showed a stabilizing effect on the secondary structural elements of both amide I and amide III bands. Whey protein isolate dispersions in water were also characterized by transmission electron microscopy by a spherical shape with 2 populations (6 and 70 nm). Salt increase alone resulted in the formation of denser aggregates, whereas a transition from spherical/compact protein aggregates to linear ones was observed due to combined salt/heat effect. The important size of these edifices was confirmed by microscopy and light-scattering techniques. Moreover, protein surface hydrophobicity related to the number of hydrophobic sites available decreased significantly. Finally, experimental results demonstrated the strong interaction between ionic strength and dynamic thermal treatment on protein functional properties and their careful adjustment could enable the food industry to effectively use WPI as a gelling agent.

Toward a better determination of dairy powders surface composition through XPS matrices development

The surface composition of dairy powders prepared by mixing various amounts of micellar casein (MC), whey proteins isolate (WPI), lactose, and anhydrous milk fat (AMF) was investigated by XPS measurements. The use of matrices are generally accepted to transform surface atomic composition (i.e., C, O, N contents) into surface component composition (i.e., lactose, proteins, lipids). These atomic-based matrices were revisited and two new matrices based on the surface bond composition were developed. Surface compositions obtained from atomic and bond-based matrices were compared. A successful matrix allowing good correlations between XPS predicted and theoretical surface composition for powders free from fat was identified. Nevertheless, samples containing milk fat were found to present a possible segregation of components owing to the AMF overrepresentation on the surface. Supplementary analyses (FTIR, SEM) were carried out in order to investigate the homogeneity of the mixtures.

Impacts of pH-mediated EPS structure on probiotic bacterial pili–whey proteins interactions

Probiotic bacteria are routinely incorporated into dairy foods because of the health benefits they can provide when consumed. In this work, the marked pH-dependence of the pili/EPS organization at the outer surface of Lactobacillus rhamnosus GG is characterized in detail by Single Cell Force Microscopy and cell electrophoretic mobility measurements analyzed according to formalisms for nanomechanical contact and soft particle electrokinetics, respectively. At pH 6.8, LGG pili are easily accessible by AFM tips functionalized with whey proteins for specific binding, while at pH 4.8 the collapsed EPS surface layer significantly immobilized the LGG pili. This resulted in their reduced accessibility to the specific whey-coated AFM tip, and to stronger whey protein-pili rupture forces. Thus, pili interactions with whey proteins are screened to an extent that depends on the pH-mediated embedment of the pili within the EPS layer.