KINETIC STUDY OF THE pH INFLUENCE ON BSA THERMAL DENATURATION
نویسنده
چکیده
BSA solution and the buffer used as a solvent, A is the area of the V = f(T) plot obtained for a given step of the considered thermal denaturation process and a is the part of this surface corresponding to a given temperature T. In this study some conformational changes induced by thermal denaturation of BSA macromolecule were evidenced, the temperatures of transition as well as the # G values for the first transition being presented and discussed.
منابع مشابه
The Effect of TiO2-Nanoparticle on the Activity and Stability of Trypsin in Aqueous Medium
Trypsin (E.C.3.4.21.4) is a serine protease commonly used in proteomics for digestion of proteins. In the present study, the effect of nano-TiO2 on the conformation and catalytic activity of trypsin were studied. The thermal denaturation of trypsin has been investigated in the presence and absence of nano-TiO2 over the temperature range (293-373 K) at pH 3.0 and 7.25, using temperature scanning...
متن کاملCalorimetric Study of Thermal Denaturation of (3-Lactoglobulin
Effects of pH and milk constituents (milk ultrafiltrate and ~:-casein) on denaturation of fl-lactoglobulin were investigated by a dynamic method based on differential scanning calorimetry. The apparent reaction order of /Ltactoglobulin denaturation by the dynamic method was 2.0 over the pH range of 4.0 to 9.0, which is in fair agreement with results by other investigators using more classical m...
متن کاملDenaturation studies on bovine serum albumin–bile salt system: Bile salt stabilizes bovine serum albumin through hydrophobicity
Protein denaturation is under intensive research, since it leads to neurological disorders of severe consequences. Avoiding denaturation and stabilizing the proteins in their native state is of great importance, especially when proteins are used as drug molecules or vaccines. It is preferred to add pharmaceutical excipients in protein formulations to avoid denaturation and thereby stabilize the...
متن کاملThermal stability of peroxidase from Chamaerops excelsa palm tree at pH 3.
The structural stability of a peroxidase, a dimeric protein from palm tree Chamaerops excelsa leaves (CEP), has been characterized by high-sensitivity differential scanning calorimetry, circular dichroism and steady-state tryptophan fluorescence at pH 3. The thermally induced denaturation of CEP at this pH value is irreversible and strongly dependent upon the scan rate, suggesting that this pro...
متن کاملRheological Characterization Bovine Serum Albumin Gels Induced by High Hydrostatic Pressure
Similarly to heating, non-thermal technologies like High Hydrostatic Pressure (HHP) are able to affect the native conformation of proteins, causing denaturation, aggregation or gelation. The aim of this work is to evaluate the effect of product’s chemical-physical characteristics, namely pH and protein concentration, and process parameters, namely pressure level and processing time, on the stab...
متن کامل