Effects of protein and phosphate buffer concentrations on thermal denaturation of lysozyme analyzed by isoconversional method
| Autor: | Yongxiang Liu, X.M. Cao, Y. Tian, Zhongchi Wang, Cunxin Wang |
|---|---|
| Rok vydání: | 2016 |
| Předmět: |
Thermal denaturation
Protein Denaturation Hot Temperature Bioengineering 02 engineering and technology Buffers 010402 general chemistry 01 natural sciences Applied Microbiology and Biotechnology Phosphates chemistry.chemical_compound Differential scanning calorimetry Horizontal scan rate Chromatography Calorimetry Differential Scanning Phosphate buffered saline technology industry and agriculture Proteins General Medicine Hydrogen-Ion Concentration Models Theoretical 021001 nanoscience & nanotechnology 0104 chemical sciences Biochemistry chemistry Muramidase Lysozyme 0210 nano-technology Protein concentration Research Paper Biotechnology |
| Zdroj: | Bioengineered. 7:235-240 |
| ISSN: | 2165-5987 2165-5979 |
| DOI: | 10.1080/21655979.2016.1197629 |
| Popis: | Thermal denaturation of lysozymes was studied as a function of protein concentration, phosphate buffer concentration, and scan rate using differential scanning calorimetry (DSC), which was then analyzed by the isoconversional method. The results showed that lysozyme thermal denaturation was only slightly affected by the protein concentration and scan rate. When the protein concentration and scan rate increased, the denaturation temperature (Tm) also increased accordingly. On the contrary, the Tm decreased with the increase of phosphate buffer concentration. The denaturation process of lysozymes was accelatated and the thermal stability was reduced with the increase of phosphate concentration. One part of degeneration process was not reversible where the aggregation occurred. The other part was reversible. The apparent activation energy (Ea) was computed by the isoconversional method. It decreased with the increase of the conversion ratio (α). The observed denaturation process could not be described by a simple reaction mechanism. It was not a process involving 2 standard reversible states, but a multi-step process. The new opportunities for investigating the kinetics process of protein denaturation can be supplied by this novel isoconversional method. |
| Databáze: | OpenAIRE |
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