When microalgae are simultaneously applied for wastewater treatment and lipid production, soluble algal products (SAP) should be paid much attention, as they are important precursors for formation of disinfection byproducts (DBPs), which have potential risks for human health. Chlorella sp. HQ is an oleaginous microalga that can generate SAP during growth, especially in the exponential phase. This study investigated the contribution of SAP from Chlorella sp. HQ to DBP formation after chlorination. The predominant DBP precursors from SAP were identified with the 3D excitation-emission matrix fluorescence. After chlorination, a significant reduction was observed in the fluorescence intensity of five specific fluorescence regions, particularly aromatic proteins and soluble microbial by-product-like regions, accompanied with slight shifting of the peak. The produced DBPs were demonstrated to include trihalomethanes and haloacetic acids. As the algal cultivation time was extended in wastewater, the accumulated SAP strengthened the formation of DBPs. The trend for DBP formation was as follows: chloroform>dichloroacetic acid>trichloroacetic acid.
Antibiotics are widely used in daily life but their abuse has posed a potential threat to human health. To evaluate the toxicity of chloramphenicol (CAP) at the protein level, the interaction between CAP and human serum albumin (HSA) was investigated by fluorescence, Ultraviolet–visible (UV–Vis) absorption, Fourier transform infrared (FT-IR) spectroscopy and molecular docking methods. Fluorescence data revealed that the fluorescence quenching of HSA by CAP was the result of the formation of CAP–HSA complex, and the binding constant was determined to be 3.196?×?104 L mol?1 at 310 K. The thermodynamic determination indicated that the interaction was driven by enthalpy change and entropy change together, where the multiple hydrogen bonds (CAP and the residues Arg 222 and His 242 of HSA) and van der Waals forces were the dominant binding force. The site marker competition revealed that CAP bound into sub-domain IIA of HSA. The binding of CAP induced the drastic reduction in α-helix conformation and the significant enhancement in β-sheet conformation of HSA. Molecular docking study further confirmed the binding mode obtained by experimental study. This work provides a new quantitative evaluation method for antibiotics to cause the protein damage. 相似文献