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Abstract
The enthalpy changes of salting process of hen-egg white lysozyme in buffer acetate solutions (pH=4.25) as a function of concentration of following electrolytes: LiCl, KCl, K2SO4, Li2 SO4 and (NH4)2SO4 are determined. Obtained data according to McMillan and Mayer’s approach, has been analyzed in the terms of the enthalpic pairwise interaction coefficients: lysozyme – lysozyme h xx, and lysozyme – salt h xy. The ability of cations to precipitate lysozyme solution in relation to the concentration of cations can be seen from the series as follows: Li+> Na+>K+>NH4++
Abstract
To reveal the denaturation mechanism of lysozyme by dimethyl sulfoxide (DMSO), thermal stability of lysozyme and its preferential solvation by DMSO in binary solutions of water and DMSO was studied by differential scanning calorimetry (DSC) and using densities of ternary solutions of water (1), DMSO (2) and lysozyme (3) at 298.15 K. A significant endothermic peak was observed in binary solutions of water and DMSO except for a solution with a mole fraction of DMSO (x 2) of 0.4. As x 2 was increased, the thermal denaturation temperature T m decreased, but significant increases in changes in enthalpy and heat capacity for denaturation, ΔH cal and ΔC p, were observed at low x 2 before decreasing. The obtained amount of preferential solvation of lysozyme by DMSO (∂g 2/∂g 3) was about 0.09 g g−1 at low x 2, indicating that DMSO molecules preferentially solvate lysozyme at low x 2. In solutions with high x 2, the amount of preferential solvation (∂g 2/∂g 3) decreased to negative values when lysozyme was denatured. These results indicated that DMSO molecules do not interact directly with lysozyme as denaturants such as guanidine hydrochloride and urea do. The DMSO molecules interact indirectly with lysozyme leading to denaturation, probably due to a strong interaction between water and DMSO molecules.
Summary
Calorimetric determination of the total enthalpy changes (ΔH i) of guanidine-denatured lysozyme (Lys) during the adsorption with simultaneously refolding on the surface of hydrophobic interaction chromatography packings was carried out at 250.001C. The measured ΔH iin the circumstances should include the changes in the three fractions: adsorption, dehydration and molecular conformation. It was found that when the unfolded Lys molecules are adsorbed and refold on the surface, entropy-driving caused by the dehydration of Lys mainly dominates the foregoing process. The refolding enthalpies of Lys, ΔΔH iwere found to be 10~100 folds higher than that measured in usual solutions.</o:p>
Abstract
The interactions of lysozyme and myoglobin with anionic surfactants (hydrogenated and fluorinated), at surfactant concentrations below the critical micelle concentration, in aqueous solution were studied using spectroscopic techniques. The temperature conformational transition of globular proteins by anionic surfactants was analysed as a function of denaturant concentration through absorbance measurements at 280 nm. Changes in absorbance of protein-surfactant system with temperature were used to determine the unfolding thermodynamics parameters, melting temperature, T m, enthalpy, ΔH m, entropy, ΔS m and the heat capacity change, ΔC p, between the native and denatured states.
Abstract
Calorimetric measurement of adsorption enthalpies of native lysozyme(Lyz) on a moderately hydrophobic surface at 25°C, pH 7.0 and various salt concentrations was performed. Based on the thermodynamics of stoichiometric displacement theory (SDT), we calculated the fractions of thermodynamic functions involving four subprocesses during a displacement adsorption process from the directly determined enthalpies in combination with adsorption isotherm measurements. The thermodynamic fractions reveal the relative degree of the four subprocesses for contributions to enthalpy, entropy and free energy. The results show that native Lyz adsorption on a moderately hydrophobic surface is an entropy driven process contributed mainly by conformational loss of adsorbed Lyz.
Abstract
Heat effects and densities of hen egg lysozyme in the phosphate buffer at pH 8.8 and various NaCl concentrations were determined at 25°C by LKB 10700-2 microcalorimeter and an Anton Paar 60/602 densimeter. The relation between the changes of the enthalpy and apparent molar volumes vs. molality of NaCl were determined. The data are discussed together with the data obtained previously for hen egg lysozyme solutions with NaCl salt in Na-acetate buffer pH 4.2.
Interaction of a homologous series of n-alkyl trimethyl ammonium bromides with eggwhite lysozyme
Microcalorimetric and spectroscopic study
Abstract
The interaction of a series of n-alkyl trimethyl ammonium bromides (C12, C14 and C16) with egg white lysozyme have been studied using fluorescence and UV-Vis spectroscopies and isothermal titration calorimetry (ITC). The trend of variation of molar absorptivity at 281 nm, quantum yields (λex=281 nm) and heat of interaction with respect to surfactant concentration, were measured. The spectrophotometric results show that the hydrophobic interactions have a major role in denaturation mechanism and it would be increased with increasing in hydrocarbon tail length of surfactant. The ITC results indicated the two-step mechanism for unfolding of lysozyme due to its interaction with surfactants.
Abstract
Both calorimetric determination of displacement adsorption enthalpies ΔH and measurement of adsorbed amounts of lysozyme (Lyz) denatured by 1.8 mol L−1 guanidine hydrochloride (GuHCl) on a moderately hydrophobic packings at 298 K, pH 7.0 and various salt concentrations were carried out. Based on the thermodynamics of stoichiometric displacement theory (SDT) the fractions of thermodynamic functions, which related to four subprocesses of denatured protein refolding on the surface, were calculated and thermodynamic analysis that which one of the subprocesses plays major role for contribution to the thermodynamic fractions was made in detail. The moderately hydrophobic surface can provide denatured Lyz energy and make it gain more conformation with surface coverage or salt concentration increment. The displacement adsorptions of denatured Lyz onto PEG-600 surface are exothermic, more structure-ordered and enthalpy driven processes.
alone and in combination as well ( Kim et al., 1995 ). Collagen-lysozyme was found to be effective in suppressing bacteria on salmon ( Wang et al., 2017 ). Lysozyme, 0.5% solution, was able to reduce surface spoilage of carp ( Palotás et al., 2020
. 4. Callewaert , L. , Michiels , C. W. ( 2010 ) Lysozymes in the animal kingdom . J. Biosci. 35 , 127 – 160 . 5
