We studied the role played by temperature and rennet concentration in the coagulation process for cheese manufacture and the evaluation of their kinetics. We concluded that temperature is the main factor that determines the kinetics. The rennet concentration was unimportant probably due to the fast action of the enzyme chymosin. The Dynamic light scattering technique allowed measuring the aggregate's size and their formation kinetics. The volume fraction of solids was determined from viscosity measurements, showing profiles that are in agreement with the size profiles. The results indicate that the formation of the aggregates for rennet cheese is strongly dependent on temperature and rennet concentration. The results revealed that at 35·5 °C the volume fraction of solids has the maximum slope, indicating that at this temperature the curd is formed rapidly. The optimal temperature throughout the process was established. Second-order kinetics were obtained for the process. We observed a quadratic dependence between the rennet volume and the volume fraction of solids (curd), thereby indicating that the kinetics of the curd production should be of order two.

Nominal compositions of In2Ti1−xTmxO5−δ, (0.0 ≤ x ≤ 0.2 and Tm = Fe3+ and Cr3+) were synthesized by ceramic route and characterized by relevant techniques. In2Ti1−xFexO5−δ samples were single phased isomorphic with In2TiO5 phase while Cr substitution has resulted in mixed phased compositions. Dynamic light scattering experiments showed the increase in proportion of smaller sized particles with the increase in extent of Fe substitution. Mössbauer spectra revealed that Fe exists in +3 oxidation state in substituted oxides. The band gap decreased from 3.2 (In2TiO5) to 2.1 eV (In2Ti0.8Fe0.2Ox−δ) and to 1.9 eV in case of Cr substitution (In2Ti0.8Cr0.2O5−δ) attributed to participation of Fe 3d/Cr 3d levels. Photocatalytic H2 generation was evaluated over the substituted oxides from water–methanol mixtures under UV–visible irradiation. The decreasing order of photocatalytic activity is as follows: 20% Fe (mol%) > 10% Fe > indium titanate ≈ 20% Cr > 10% Cr. The loading of Pt as cocatalyst on surface of most active photocatalyst, In2Ti0.8Fe0.2Ox−δ further enhanced the photocatlytic H2 yield.

The Nef protein of human immunodeficiency virus type I (HIV-1) is an important determinant for the onset of AIDS disease. The self-association properties of HIV-1 Nef are analyzed by chemical cross-linking, dynamic light scattering, equilibrium analytical ultracentrifugation, and NMR spectroscopy. The experimental data show that the HIV-1 Nef core domain forms stable homo-dimers and trimers in solution, but not higher oligomers. These Nef homomers are not covalently linked by disulfide bridges, and the equilibrium between these forms is dependent on the Nef concentration. We further provide the molecular basis for the Nef core dimers and trimers obtained by analysis of crystallographic models. Oligomerization of biological polypeptides is a common tool used to trigger events in cellular signaling and endocytosis, both of which are targeted by Nef. The quaternary structure of Nef may be of physiological importance and may help to connect its cellular targets or to increase affinity of the viral molecule for its ligands. The herein described models for Nef dimers and trimers will allow further mutational studies to elucidate their role in vivo. These results provide novel insight into the structural and functional relationships of this important viral protein. Moreover, the oligomer interface may represent a novel target for the design of antiviral agents.

The trifluoroethanol (TFE)-induced structural changes of two proteins widely used in folding experiments, bovine α-lactalbumin, and bovine pancreatic ribonuclease A, have been investigated. The experiments were performed using circular dichroism spectroscopy in the far- and near-UV region to monitor changes in the secondary and tertiary structures, respectively, and dynamic light scattering to measure the hydrodynamic dimensions and the intermolecular interactions of the proteins in different conformational states. Both proteins behave rather differently under the influence of TFE: α-lactalbumin exhibits a molten globule state at low TFE concentrations before it reaches the so-called TFE state, whereas ribonuclease A is directly transformed into the TFE state at TFE concentrations above 40% (v/v). The properties of the TFE-induced states are compared with those of equilibrium and kinetic intermediate states known from previous work to rationalize the use of TFE in yielding information about the folding of proteins. Additionally, we report on the properties of TFE/water and TFE/buffer mixtures derived from dynamic light scattering investigations under conditions used in our experiments.