Exploring whey and faba bean protein interactions at the oil-water interface: A combined drop tensiometry and microfluidicsstudy.

The interfacial properties of model oil-water interfaces stabilized by faba bean protein isolate (FPI), whey protein isolate (WPI), and their mixtures were investigated. Two complementary techniques, microfluidics-based analysis and drop tensiometry were employed to study the impact of protein mixing on interfacial tension, adsorption kinetics, and droplet stability. A microfluidic platform was used for droplet generation and single droplet analysis, assessing the impact of protein blending on droplet size and shape eccentricity after droplet generation.

FTIR Imaging as a Tool for Studying Protein Dynamics and Interactions at the Oil/Water Interface with Spatial Resolution: A Single Droplet Analysis Approach.

Emulsions play a pivotal role in the food, pharmaceutical, and cosmetic industries due to their unique structural properties and versatility in delivering active ingredients. Developing emulsion systems with optimized structural and functional properties is a key focus, requiring a comprehensive understanding of their physicochemical attributes. A major challenge in emulsion research is accurately characterizing the molecular-level interactions at the interface, which are critical for stability, performance, and functionality.

A simple and robust method for laboratory-scale preparation of butter.

The aim of this study was to develop a small-scale model system resembling the micro- and meso-structure of butter, namely having a water droplet size distribution and water content close to that of commercially produced butter. Although it is possible to churn cream on a small scale, matching the microstructure of butter is a challenge. A 2-step churning process was introduced with the application of a kitchen mixer.

single-droplet analysis of emulsified fat using confocal Raman microscopy: insights into crystal network formation within spatial resolution.

Fat crystallization is one of the predominant factors influencing the structure and properties of fat-containing emulsions. In the present study, the role of emulsifiers on fat crystallization dynamics within droplet multiphase systems was evaluated single-droplet analysis, taking advantage of the non-destructive properties of confocal Raman microscopy. Palm oil droplets dispersed in water were used as a model system, due to palm oil's well-known crystallization properties.

Formation and physicochemical properties of glycogen phosphorylase in complex with a cationic polyelectrolyte.

The accumulation of rabbit muscle glycogen phosphorylase b (RMGPb) in electrostatic complexes with the cationic polyelectrolyte poly 2-(dimethylamino) ethyl methacrylate in its quenched form (QPDMAEMA) was studied in two buffer solutions. In the N-bis(2-hydroxyethyl)-2-aminoethanesulfonic acid (BES) buffer, large complexes of RMGPb-QPDMAEMA were formed which adopted smaller sizes as QPDMAEMA concentration increased. However, in N-(2-hydroxyethyl)piperazine-N'-(2-ethanesulfonic acid) (HEPES) buffer, the hydrodynamic radius of the formed complexes gradually increased as the polymer concentration increased.

A glucose-based molecular rotor inhibitor of glycogen phosphorylase as a probe of cellular enzymatic function.

Molecular rotors belong to a family of fluorescent compounds characterized as molecular switches, where a fluorescence on/off signal signifies a change in the molecule's microenvironment. Herein, the successful synthesis and detailed study of ()-2-cyano-3-(-(dimethylamino)phenyl)--(β-D-glucopyranosyl)acrylamide (RotA), is reported. RotA was found to be a strong inhibitor of rabbit muscle glycogen phosphorylase (RMGP), that binds at the catalytic site of the enzyme.

Synthesis, Kinetic and Conformational Studies of 2-Substituted-5-(β-d-glucopyranosyl)-pyrimidin-4-ones as Potential Inhibitors of Glycogen Phosphorylase.

Dysregulation of glycogen phosphorylase, an enzyme involved in glucose homeostasis, may lead to a number of pathological states such as type 2 diabetes and cancer, making it an important molecular target for the development of new forms of pharmaceutical intervention. Based on our previous work on the design and synthesis of 4-arylamino-1-(β-d-glucopyranosyl)pyrimidin-2-ones, which inhibit the activity of glycogen phosphorylase by binding at its catalytic site, we report herein a general synthesis of 2-substituted-5-(β-d-glucopyranosyl)pyrimidin-4-ones, a related class of metabolically stable, glucosyl-based, analogues. The synthetic development consists of a metallated heterocycle, produced from 5-bromo-2-methylthiouracil, in addition to protected d-gluconolactone, followed by organosilane reduction.