A Biocompatible, pH-Sensitive, and Magnetically Separable Superparamagnetic Hydrogel Nanocomposite as an Efficient Platform for the Removal of Cationic Dyes in Wastewater Treatment.

A series of environment-friendly cationic dye adsorbents, namely, pH-sensitive superparamagnetic hydrogel nanocomposite AA-VSA-P/SPIONs systems with different concentrations of superparamagnetic iron oxide nanoparticles (SPIONs; 1.2, 3.2, and 5.2 wt %), was synthesized by free-radical polymerization reaction using two pH-sensitive monomers, acrylic acid (AA) and vinylsulfonic acid (VSA), in an optimum ratio, in the presence of presynthesized SPIONs. The structural properties, thermal stability, and chemical configuration of AA-VSA-P/SPIONs systems with different weight percentages of SPIONs were characterized by XRD, TGA, Raman spectroscopy, and FTIR spectroscopy. The systems show substantial efficiency as dye adsorbents for removing cationic dyes (MB dye) from aqueous solution in neutral to alkaline medium. Further, these systems exhibit easy magnetic separation capabilities from aqueous solutions after dye adsorption, even for a very low weight percentage of SPIONs. The adsorption kinetics, mechanism, and isotherms of these systems were evaluated. The study suggests consistency with the pseudo-second-order kinetic model, following an intraparticle diffusion mechanism, where the heterogeneous surface of the system having different activation energies for adsorption plays the crucial role in dye adsorption via chemisorption for higher pH medium, which was further substantiated by excellent data fit with the Freundlich isotherm model. Biocompatibility and regeneration-ability studies establish the environment-friendliness and cost effectivity of the system.

Crystallization and preliminary X-ray diffraction analysis of Xaa-Pro dipeptidase from Xanthomonas campestris.

Xaa-Pro dipeptidase (XPD; prolidase; EC 3.4.13.9) specifically hydrolyzes dipeptides with a prolyl residue at the carboxy-terminus. Xanthomonas spp. possess two different isoforms of XPD (48 and 43 kDa) which share ∼24% sequence identity. The XPD of 43 kDa in size (XPD43) from Xanthomonas spp. is unusual as it lacks the strictly conserved tyrosine residue (equivalent to Tyr387 in Escherichia coli aminopeptidase P) that is suggested to be important in the proton-shuttle transfer required for catalysis in the M24B (MEROPS) family. Here, the crystallization and preliminary X-ray analysis of XPD43 from X. campestris (GenBank accession No. NP_637763) are reported. Recombinant XPD43 was crystallized using the microbatch-under-oil technique. Diffraction data were collected on the recently commissioned protein crystallography beamline (PX-BL21) at the Indian synchrotron (Indus-2, 2.5 GeV) to 1.83 Šresolution with 100% completeness. The crystal belonged to space group P212121, with unit-cell parameters a = 84.32, b = 105.51, c = 111.35 Å. Two monomers are expected to be present in the asymmetric unit of the crystal, corresponding to a solvent content of 58%. Structural analysis of XPD43 will provide new insights into the role of the conserved residues in catalysis in the M24B family.

Expression, purification, crystallization and preliminary X-ray diffraction analysis of acylpeptide hydrolase from Deinococcus radiodurans.

Acylpeptide hydrolase (APH; EC 3.4.19.1), which belongs to the S9 family of serine peptidases (MEROPS), catalyzes the removal of an N-acylated amino acid from a blocked peptide. The role of this enzyme in mammalian cells has been suggested to be in the clearance of oxidatively damaged proteins as well as in the degradation of the ß-amyloid peptides implicated in Alzheimer's disease. Detailed structural information for the enzyme has been reported from two thermophilic archaea; both of the archaeal APHs share a similar monomeric structure. However, the mechanisms of substrate selectivity and active-site accessibility are totally different and are determined by inter-domain flexibility or the oligomeric structure. An APH homologue from a bacterium, Deinococcus radiodurans (APHdr), has been crystallized using microbatch-under-oil employing the random microseed matrix screening method. The protein crystallized in space group P21, with unit-cell parameters a = 77.6, b = 189.6, c = 120.4 Å, ß = 108.4°. A Matthews coefficient of 2.89 Å(3) Da(-1) corresponds to four monomers, each with a molecular mass of ∼73 kDa, in the asymmetric unit. The APHdr structure will reveal the mechanisms of substrate selectivity and active-site accessibility in the bacterial enzyme. It will also be helpful in elucidating the functional role of this enzyme in D. radiodurans.