Selective degradation of tetracycline antibiotics present in raw milk by electrochemical method.

The dairy industry disposes of a large volume of waste milk with antibiotic residues, which is a great cause of much concern in soil and water environments. In this study, the electrochemical oxidation of tetracycline antibiotics (TCs) in cow's milk was investigated. Milk contains a high concentration of organic matter, and the concentrations of TCs residues are extremely low. The effects of anode materials and electrolytes on the degradation of oxytetracycline (OTC) were investigated. A higher degradation rate for the OTC was attained using the inactive anode or a NaCl electrolyte. It was found that a physically adsorbed oxidant on the surface of the anode and indirect oxidation using electrogenerated hypochlorite could enhance the degradation of OTC in raw milk. The organic components in milk samples affected the removal rate of the OTC. The removal rate constants for the OTC in raw milk were 2.8-7.7 times higher than the chemical oxygen demand values. It was found that electrochemical oxidation could decompose low concentrations of TCs in high concentrations of organic matter solutions selectively. The results indicate that electrochemical oxidation is an effective method for the treatment of TCs in waste milk.

Prion protein fate governed by metal binding.

The conversion of the normal cellular prion protein to an abnormal isoform is considered to be causal to the prion diseases or transmissible spongiform encephalopathies. The prion protein is a copper binding protein but under some conditions may bind other metals. In particular, the binding of manganese has been suggested to convert the prion protein (PrP) to a protease resistant isoform. Therefore, the differences in the way the protein binds copper and manganese might be revealing in terms of the mechanism of conversion of the protein or its normal cellular activity. We report the use of near-infrared spectroscopy for studies on aqueous solutions of prion protein binding Cu or Mn. These alloforms of the protein were analyzed by spectral data acquisition and multivariate analysis. Our results indicate that PrP binds both Mn and Cu differently. Analyses of Cu binding suggest that the PrP-Cu complex protected Cu from the water increasing protein stability. PrP-Mn does not protect Mn from water interactions. A real-time study of the protein alloforms showed that PrP-Cu remains stable in solution, but that PrP-Mn underwent highly different changes that led to fibril formation.