Studying the denaturation of bovine serum albumin by a novel approach of difference-UV analysis
| Autor: | Thomas Moschakis, Athanasios Nikolaidis |
|---|---|
| Rok vydání: | 2016 |
| Předmět: |
0301 basic medicine
Protein Denaturation Hot Temperature Hydrochloride 010402 general chemistry 01 natural sciences Analytical Chemistry 03 medical and health sciences chemistry.chemical_compound symbols.namesake Differential scanning calorimetry Animals Denaturation (biochemistry) Bovine serum albumin Guanidine Arrhenius equation Chromatography Protein molecules biology Calorimetry Differential Scanning Spectrum Analysis Temperature Serum Albumin Bovine General Medicine 0104 chemical sciences Denaturation midpoint Kinetics 030104 developmental biology chemistry Biochemistry symbols biology.protein Cattle Food Science |
| Zdroj: | Food chemistry. 215 |
| ISSN: | 1873-7072 |
| Popis: | A novel approach in the analysis of difference-UV spectrophotometric data for determining the heat denaturation degree of bovine serum albumin (BSA) was assessed. Five different parameters of difference-UV spectra were obtained by subtracting spectra of unheated and denatured protein solutions at different temperature-time combinations. BSA was found to exhibit a maximum degree of heat denaturation of about 17% compared to the complete unfolding caused by 6M guanidine hydrochloride. This low degree of heat denaturation is probably caused by the aggregation of the initially unfolded protein molecules. The kinetic analysis exhibited discontinuities in the Arrhenius plots, distinguishing the unfolding and aggregation phases of the denaturation process, whereas such a discrimination could not be obtained by differential scanning calorimetry analyses. The proposed method is accurate, fast, simple and sensitive enough to detect changes in the protein heat denaturation even at short temperature-time intervals. |
| Databáze: | OpenAIRE |
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