C-phycocyanin production with high antioxidant activity of a new thermotolerant freshwater Desertifilum tharense UAM-C/S02 strain.

A native cyanobacterial strain, Desertifilum tharense UAM-C/S02, was studied as a possible C-phycocyanin (C-PC) producer. Photosynthetic activity (PA) assays through oxygen production determined the proper temperature and range of irradiances to be tested in a stirred tank photobioreactor. The highest C-PC productivity (97 mg L-1 d-1), with a yield of 86.46 mgC-PC gB-1 was obtained at 730 µmol photons m-2 s-1 with a biomass productivity of 608 mg L-1 d-1 and the CO2 fixation rate was 1,194  mg L-1 d-1. The 1.81 crude extract purity value is the highest reported for this genus, which was improved to biomarker-grade purity after a two-step purification strategy comprising precipitation with ammonium sulfate, followed by dialysis. The purified C-PC was almost entirely radical-free using 1 mg mL-1, which validates its potential use in therapeutic formulations.

Sodium Alginate/Chitosan Scaffolds for Cardiac Tissue Engineering: The Influence of Its Three-Dimensional Material Preparation and the Use of Gold Nanoparticles.

Natural biopolymer scaffolds and conductive nanomaterials have been widely used in cardiac tissue engineering; however, there are still challenges in the scaffold fabrication, which include enhancing nutrient delivery, biocompatibility and properties that favor the growth, maturation and functionality of the generated tissue for therapeutic application. In the present work, different scaffolds prepared with sodium alginate and chitosan (alginate/chitosan) were fabricated with and without the addition of metal nanoparticles and how their fabrication affects cardiomyocyte growth was evaluated. The scaffolds (hydrogels) were dried by freeze drying using calcium gluconate as a crosslinking agent, and two types of metal nanoparticles were incorporated, gold (AuNp) and gold plus sodium alginate (AuNp+Alg). A physicochemical characterization of the scaffolds was carried out by swelling, degradation, permeability and infrared spectroscopy studies. The results show that the scaffolds obtained were highly porous (>90%) and hydrophilic, with swelling percentages of around 3000% and permeability of the order of 1 × 10−8 m2. In addition, the scaffolds proposed favored adhesion and spheroid formation, with cardiac markers expression such as tropomyosin, troponin I and cardiac myosin. The incorporation of AuNp+Alg increased cardiac protein expression and cell proliferation, thus demonstrating their potential use in cardiac tissue engineering.

Squalene-Rich Amaranth Oil Pickering Emulsions Stabilized by Native α-Lactalbumin Nanoparticles.

The stabilization of Pickering emulsions by nanoparticles has drawn great interest in the field of food science and technology. In this study, α-Lactalbumin nanoparticles prepared by the desolvation and cross-linking method from protein solutions with initial pH values of 9 and 11 were used to stabilize squalene-rich amaranth oil Pickering o/w emulsions. The effect of different concentrations of nanoparticles on the size, size distribution, ζ potential, and emulsion stability was evaluated using dynamic light scattering, electron microscopy, and light backscattering. Dependence of the emulsions' droplet size on the nanoparticle concentration was observed, and the critical coverage ratio was reached when 5-10% nanoparticles concentration was used. Our findings suggest that α-LA nanoparticles at a 10% concentration can be used as novel stabilizers for Pickering emulsions to provide protection for beneficial lipophilic bioactive compounds. This is the first time that native α-LA nanoparticles have been used as stabilizers of Pickering emulsions.

Characterization of flavonoid-protein interactions using fluorescence spectroscopy: Binding of pelargonidin to dairy proteins.

In this study, the interaction between the flavonoid pelargonidin and dairy proteins: ß-lactoglobulin (ß-LG), whey protein (WPI), and caseinate (CAS) was investigated. Fluorescence experiments demonstrated that pelargonidin quenched milk proteins fluorescence strongly. However, the protein secondary structure was not significantly affected by pelargonidin, as judged from far-UV circular dichroism. Analysis of fluorescence data indicated that pelargonidin-induced quenching does not arise from a dynamical mechanism, but instead is due to protein-ligand binding. Therefore, quenching data were analyzed using the model of independent binding sites. Both ß-LG and CAS, but not WPI, showed hyperbolic binding isotherms indicating that these proteins firmly bound pelargonidin at both pH 7.0 and 3.0 (binding constants ca. 1.0×10(5) at 25.0°C). To investigate the underlying thermodynamics, binding constants were determined at 25.0, 35.0, and 45.0°C. These results pointed to binding processes that depend on the structural conformation of the milk proteins.

Deconvolution of complex differential scanning calorimetry profiles for protein transitions under kinetic control.

A frequent outcome in differential scanning calorimetry (DSC) experiments carried out with large proteins is the irreversibility of the observed endothermic effects. In these cases, DSC profiles are analyzed according to methods developed for temperature-induced denaturation transitions occurring under kinetic control. In the one-step irreversible model (native → denatured) the characteristics of the observed single-peaked endotherm depend on the denaturation enthalpy and the temperature dependence of the reaction rate constant, k. Several procedures have been devised to obtain the parameters that determine the variation of k with temperature. Here, we have elaborated on one of these procedures in order to analyze more complex DSC profiles. Synthetic data for a heat capacity curve were generated according to a model with two sequential reactions; the temperature dependence of each of the two rate constants involved was determined, according to the Eyring's equation, by two fixed parameters. It was then shown that our deconvolution procedure, by making use of heat capacity data alone, permits to extract the parameter values that were initially used. Finally, experimental DSC traces showing two and three maxima were analyzed and reproduced with relative success according to two- and four-step sequential models.

Correction: Microencapsulation of probiotics in hydrogel particles: enhancing Lactococcus lactis subsp. cremoris LM0230 viability using calcium alginate beads.

Correction for 'Microencapsulation of probiotics in hydrogel particles: enhancing Lactococcus lactis subsp. cremoris LM0230 viability using calcium alginate beads' by Timothy W. Yeung et al., Food Funct., 2016, 7, 1797-1804.

Microencapsulation of probiotics in hydrogel particles: enhancing Lactococcus lactis subsp. cremoris LM0230 viability using calcium alginate beads.

Probiotics are beneficial microbes often added to food products to enhance the health and wellness of consumers. A major limitation to producing efficacious functional foods containing probiotic cells is their tendency to lose viability during storage and gastrointestinal transit. In this study, the impact of encapsulating probiotics within food-grade hydrogel particles to mitigate sensitivity to environmental stresses was examined. Confocal fluorescence microscopy confirmed that Lactococcus lactis were trapped within calcium alginate beads formed by dripping a probiotic-alginate mixture into a calcium solution. Encapsulation improved the viability of the probiotics during aerobic storage: after seven days, less than a two-log reduction was observed in encapsulated cells stored at room temperature, demonstrating that a high concentration of cells survived relative to non-encapsulated bacteria. These hydrogel beads may have applications for improving the stability and efficacy of probiotics in functional foods.

Application of ITC in foods: A powerful tool for understanding the gastrointestinal fate of lipophilic compounds.

BACKGROUND: Isothermal titration calorimetry (ITC) is a biophysical technique widely used to study molecular interactions in biological and non-biological systems. It can provide important information about molecular interactions (such as binding constant, number of binding sites, free energy, enthalpy, and entropy) simply by measuring the heat absorbed or released during an interaction between two liquid solutions. SCOPE OF THE REVIEW: In this review, we present an overview of ITC applications in food science, with particular focus on understanding the fate of lipids within the human gastrointestinal tract. In this area, ITC can be used to study micellization of bile salts, inclusion complex formation, the interaction of surface-active molecules with proteins, carbohydrates and lipids, and the interactions of lipid droplets. MAJOR CONCLUSIONS: ITC is an extremely powerful tool for measuring molecular interactions in food systems, and can provide valuable information about many types of interactions involving food components such as proteins, carbohydrates, lipids, surfactants, and minerals. For systems at equilibrium, ITC can provide fundamental thermodynamic parameters that can be used to establish the physiochemical origin of molecular interactions. GENERAL SIGNIFICANCE: It is expected that ITC will continue to be utilized as a means of providing fundamental information about complex materials such as those found in foods. This knowledge may be used to create functional foods designed to behave in the gastrointestinal tract in a manner that will improve human health and well-being.

α-Lactalbumin nanoparticles prepared by desolvation and cross-linking: structure and stability of the assembled protein.

A key step in the preparation of cross-linked protein nanoparticles involves the desolvation of proteins with an organic solvent, which is thought to act by modulating hydrophobic interactions. However, to date, no study has examined the conformational changes that proteins undergo during the assembly process. In this work, by using several biophysical techniques (CD spectroscopy, DSC, TEM, etc.), we studied spheroidal nanoparticles made from bovine α-lactalbumin cross-linked with glutaraldehyde in the presence of acetone. Within the nanoparticle, the polypeptide chain acquires a ß-strand-like conformation (completely different from the native protein in secondary and tertiary structure) in which several side chains likely become available for reacting with glutaraldehyde. A multiplicity of cross-linking sites, together with the polymeric nature of glutaraldehyde, may thus explain the low dry-weight fraction of protein that was found in the nanoparticles. Although covalent bonds undoubtedly constitute the main source for nanoparticle stability, noncovalent interactions also appear to play a role in this regard.