Advanced oxidation processes (AOPs) hold great promise in the removal of organic contaminants. Reactive oxygen species (ROS) produced in AOPs react with target pollutants to initially form several intermediate compounds that finally undergo complete mineralization. Such observations are reported, especially for laboratory-scale experiments performed in pure water. On the other hand, while considering real contaminated wastewater matrices, particularly industrial effluents, there are many co-existing ions. Carbonate ions are one of the major inorganic ions commonly existing in water resources. Hence, these ions have a significant impact on the respective water treatment processes. This review focused on the effect of carbonate ions on the degradation of pollutants in AOPs. In AOPs, carbonate radicals are formed by the scavenging reaction of the respective ions with ROS. The reactivity of these radicals towards the pollutant varies with respect to the structure and functionality. Therefore, depending on the functionalities of the contaminants, these ions show both positive and negative effects. Thus, this review aims to summarize the effects of carbonate species on the degradation of organic contaminants during AOPs and their environmental impacts. The carbonates enhanced the degradation of several emerging organic pollutants, including aniline, bisphenol A, rhodamine B, acid orange 7, naphthalene, and phenol derivatives. Carbonate presence was also revealed to have a positive contribution in cases of drug degradation, including sulfamethoxazole, propranolol, sulfamethazine, salbutamol, trimethoprim, azithromycin, naproxen, oxcarbazepine, and oxytetracycline.

Copper is an essential trace element for human biology where its metal dyshomeostasis accounts for an increased level of serum copper, which accelerates protein aggregation. Protein aggregation is a notable feature for many neurodegenerative disorders. Herein, we report an experimental study using two model proteins, bovine serum albumin (BSA) and human serum albumin (HSA), to elucidate the mechanistic pathway by which serum albumins get converted from a fully folded globular protein to a fibril and an amorphous aggregate upon interaction with copper. Steady-state fluorescence, time-resolved fluorescence studies, and Raman spectroscopy were used to monitor the unfolding of serum albumin with increasing copper concentrations. Steady-state fluorescence studies have revealed that the fluorescence quenching of BSA/HSA by Cu(II) has occurred through a static quenching mechanism, and we have evaluated both the quenching constants individually. The binding constants of BSA–Cu(II) and HSA–Cu(II) were found to be 2.42 × 10⁴ and 0.05 × 10⁴ M^–1, respectively. Further nanoscale morphological changes of BSA mediated by oligomers to fibril and HSA to amorphous aggregate formation were studied using atomic force microscopy. This aggregation process correlates with the Stern–Volmer plots in the absence of discernible lag phase. Raman spectroscopy results obtained are in good agreement with the increase in antiparallel β-sheet structures formed during the aggregation of BSA in the presence of Cu(II) ions. However, an increase in α-helical fractions is observed for the amorphous aggregate formed from HSA.