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Orthorhombic lysozyme solubility
1Science and Technology Corporation, Madison, AL 35758, USA.
Summary
The high-temperature orthorhombic form of chicken egg-white lysozyme exhibits lower temperature sensitivity than the tetragonal form. Its solubility decreases with increasing pH, unlike the low-temperature form.
Area of Science:
- Biochemistry
- Crystallography
- Protein Science
Background:
- Chicken egg-white lysozyme exists in different crystalline forms.
- The orthorhombic form is stable at higher temperatures (above 298 K).
- Understanding lysozyme solubility is crucial for crystallization and protein studies.
Purpose of the Study:
- To determine the solubility diagrams for the orthorhombic form of chicken egg-white lysozyme.
- To compare the solubility behavior of the orthorhombic form with the previously studied tetragonal form.
- To investigate the effects of temperature, pH, and precipitant concentration on orthorhombic lysozyme solubility.
Main Methods:
- Micro-column technique used for solubility determination.
- Solubility data collected across a pH range of 4.0 to 5.4.
- Experiments conducted within a temperature range of 297 K to 317 K.
Main Results:
- Orthorhombic lysozyme solubility increases with temperature and decreases with precipitant concentration.
- Solubility of the orthorhombic form shows less temperature sensitivity compared to the tetragonal form.
- Solubility of the orthorhombic form decreases with increasing pH, opposite to the tetragonal form.
Conclusions:
- The orthorhombic form of lysozyme has distinct solubility characteristics compared to the tetragonal form.
- Phase diagrams reveal differences in temperature and pH dependencies.
- Combined data provide insights into lysozyme's phase behavior under varying conditions.