ABSTRACT
Herein, paper mill waste sludge (PMS) from two different sources has been investigated to extract calcium hydroxide, Ca(OH)2 by a facile and inexpensive extraction process. PMS samples, collected from local paper mill plants of Bangladesh, were the main precursors wherein HCl and NaOH were used for chemical treatment. The as-synthesized products were analysed by a variety of characterization tools including X-ray diffraction (XRD), Fourier transform infrared (FTIR) spectroscopy, Raman spectroscopy, scanning electron microscopy (SEM) and energy dispersive X-ray (EDX) elemental analyses. Our studies confirm that the extracted product contains Ca(OH)2 as a major content, albeit it also includes CaCO3 phase owing to the inescapable carbonation process from the surrounding environment. The particle size of the synthesized products is in the range of 450-500 nm estimated from SEM micrographs. The crystallite domain size of the same estimated from XRD analyses and was found to be approximately 47 and 31 nm respectively for product-A and product-B considering major (101) Bragg peak of Ca(OH)2. The yield percentage of the isolated products is about 65% for samples collected from both sources.
ABSTRACT
Herein, the conductivity measurement technique is used to determine the interactions that may occur between polyvinyl pyrrolidone (PVP) polymer and cetylpyridinium chloride (CPC) surfactant in the presence of NaCl and Na2SO4 of fixed concentration at variable temperatures (298.15-323.15 K) with an interval of 5 K. In the absence or presence of salts, we observed three critical micelle concentrations (CMC) for the CPC + PVP mixture. In all situations, CMC1 values of CPC + PVP system were found to be higher in water than in attendance of salts (NaCl and Na2SO4). Temperature and additives have the tendency to affect counterion binding values. Various physico-chemical parameters were analyzed and demonstrated smoothly, including free energy (ΔG0m), enthalpy (ΔH0m) and entropy change (ΔS0m). The micellization process is achieved to be spontaneous based on the obtained negative ΔG0m values. The linearity of the ΔHmo and ΔSmo values is excellent. The intrinsic enthalpy gain (ΔH0*m) and compensation temperature (Tc) were calculated and discussed with logical points. Interactions of polymer hydrophobic chains or the polymer + surfactant associated with amphiphilic surface-active drugs can employ a strong impact on the behavior of the gels.
ABSTRACT
Herein, we have investigated the interaction of bovine serum albumin (BSA), the most abundant globular protein, with a conventional cationic surfactant, cetyldimethylethylammonium bromide (CDMEAB), through a conductivity technique in the absence/presence of electrolyte solutions at various temperatures (298.15-323.15 K). The interaction of the protein with drugs/surfactants and other additives plays a crucial role in the body. Hence, the main concern of the study is to extract the impact of BSA on surfactant molecules and vice versa. From the specific conductivity versus concentration of surfactant plots, three different noticeable critical micelle concentration (c*) values were obtained for pure CDMEAB and its mixture with protein/protein + salts. The presence of BSA and electrolytes altered the c* values of CDMEAB revealing interactions among the studied constituents where the salt solutions reduced the c* values and created a convenient environment for favorable micellization. The negative magnitudes achieved for standard free energy changes (ΔG 0 m) suggest spontaneity of micellization while the values of ΔH 0 m and ΔS 0 m signified the existence of some electrostatic and hydrophobic interactions. The values of molar heat capacity (ΔC 0 m) were positive as well as small which was an indication of less structural deformation. Molecular Dynamics (MD) simulation for all atoms revealed that the salt ions promoted non-covalent interaction between BSA and CDMEAB, and such interactions were not observed in the absence of the salt. Protein structure remained nearly same in spite of strong interaction with CDMEAB as evident from the overall RMSD (root-mean-square deviation) values of the alpha carbons and backbone of the protein and RMSF (root-mean-square fluctuation) values of the amino acid residues present in BSA. In this work thermodynamic parameters of transfer (such as ΔG 0 m.tr., ΔH 0 m.tr., and ΔC 0 p.m.tr.) were also evaluated and the results are discussed in detail. Besides, contributions of enthalpy and entropy to free energy changes were also analyzed.
