Polymerized whey protein-SDS interactions at their high concentrations.

Protein-surfactant interactions have been an ongoing topic of interest for many decades. Applications involving complexes of proteins and surfactants are relevant in food, pharmaceuticals, hygiene, molecular characterization, and other fields. In this study, the interactions of polymerized whey proteins (PWP) and sodium dodecyl sulfate (SDS) at high concentrations are investigated.

Drying kinetics and thermo-environmental analysis of a PV-operated tracking indirect solar dryer for tomato slices.

The purpose of this study is to investigate how a tracking indirect solar dryer (SD) powered by photovoltaic cells affected the drying kinetics (DK) and thermo-environmental conditions of tomato slices. In this current investigation, three air speeds (1, 1.5, and 2 m/s) are used, as well as three slice thicknesses (ST) (4, 6, and 8 mm) and two SD, one of which is integrated with fixed collector motion (FCM) and another with SD tracking collector motion (TCM).

Enzymatic cross-linking of beta-lactoglobulin: conformational properties using FTIR spectroscopy.

In this study, we use FTIR spectroscopy to probe the conformational changes of beta-lactoglobulin (beta-LG)-the main constituent of whey proteins-as subjected to enzymatic cross-linking by transglutaminase. We investigate both the amide I region (1600-1700 cm(-1)) and the C-H stretching region (2800-3100 cm(-1)). In the amide I region, spectra of denatured conformations of beta-LG, known to be necessary for cross-linking, differ according to the denaturation procedure, i.

Acid-induced gelation of enzymatically modified, preheated whey proteins.

Low-pH whey protein gels are formulated using a sequential protocol of heat treatment, enzyme incubation, and cold-set acidification. The heat-induced disulfide and enzyme-catalyzed epsilon-(gamma-glutamyl)lysine linkages, both at neutral pH, produce a polymerized protein solution. The molecular weights of these samples show an exponential increase with protein concentration.

Polymerization and gelation of whey protein isolates at low pH using transglutaminase enzyme.

Dynamic and steady shear rheology is used to examine the synthesis of low-pH (approximately 4) whey protein gels obtained through a two-step process. The first step involves cross-linking of whey proteins at pH 8 and 50 degrees C using transglutaminase enzyme, while the second step entails cold-set acidification of the resulting solution using glucono-delta-lactone (GDL) acid. During the first step, the sample undergoes enzyme-catalyzed epsilon-(gamma-glutamyl)lysine bond formation with a substantial increase in viscosity.