Removal of the Hazardous Congo Red Dye through Degradation under Visible Light Photocatalyzed by C,N Co-Doped TiO2 Prepared from Chicken Egg White.

The C,N co-doped TiO2 photocatalyst was prepared by interacting the chicken egg white having various weights (1, 2, and 4 g) with 1 g of TiO2 in an autoclave through the hydrothermal process at 150°C. The C,N co-doped TiO2 photocatalysts were characterized using Fourier transform infrared (FTIR), X-ray diffraction (XRD), specular reflectance UV/visible (SRUV/Vis), and transmission electron microscope (TEM) instruments. The photocatalytic activity of the co-doped TiO2 was evaluated by monitoring the photo-decolorization of Congo red dye under visible light through a batch experiment. The characterization results assigned that the C and N atoms from the chicken egg white have been successfully co-doped into TiO2 through interstitial and substitutional combination, which could notably narrow their band gap energy entering into the visible region. In line with the gap narrowing, the co-doping C,N into TiO2 could remarkably improve the photocatalytic activity under visible light in the dye photo-decolorization. The enhancement of the photocatalyst activity of TiO2-C,N was controlled by the weight of the egg white introduced, and 2 g of the egg white resulted in the highest activity. Further, the best dye photo-decolorization, which was about 98%, of 10 mg/L Congo red dye in 100 mL of the solution under visible irradiation could be reached by applying TiO2-C,N prepared from 2 g of the egg white, within 45 min, at pH 7, and 50 mg of the photocatalyst mass.

Poly(glycidyl methacrylate/divinylbenzene)-IDA-FeIII in phosphoproteomics.

The study of protein phosphorylation has grown exponentially in recent years, as it became evident that important cellular functions are regulated by phosphorylation and dephosphorylation of proteins on serine, threonine and tyrosine residues. The use of immobilized metal affinity chromatography (IMAC) to enrich phosphopeptides from peptide mixtures has been shown to be useful especially prior to mass spectrometric analysis. For the selective enrichment applying solid-phase extraction (SPE) of phosphorylated peptides, we introduce poly(glycidyl methacrylate/divinylbenzene) (GMD) derivatized with imino-diacetic acid (IDA) and bound Fe(III) as a material. GMD is rapidly synthesized and the resulting free epoxy groups enable an easy access to further derivatization with, e.g., IDA. Electron microscopy showed that the synthesized GMD-IDA-Fe(III) for SPE has irregular agglomerates of spherical particles. Inductively coupled plasma (ICP) analysis resulted in a metal capacity of Fe(III) being 25.4 micromol/mL. To enable on-line preconcentration and desalting in one single step, GMD-IDA-Fe(III) and Silica C18 were united in one cartridge. Methyl esterification (ME) of free carboxyl groups was carried out to prevent binding of nonphosphorylated peptides to the IMAC function. The recovery for a standard phosphopeptide using this SPE method was determined to be 92%. The suitability of the established system for the selective enrichment and analysis of model proteins phosphorylated at different amino acid residues was evaluated stepwise. After successful enrichment of beta-casein deriving phosphopeptides, the established system was extended to the analysis of in vitro phosphorylated proteins, e.g. deriving from glutathione-S-transferase tagged extracellular signal regulated kinase 2 (GST-ERK2).