The application of domestic sewage sludge (SS) may affect plant growth and soil quality through altering nutrient availability. However, the effect of SS application on the plant–soil system in sandy soils is poorly understood. In this study, we established SS application treatment plots (SL, 25 t ha⁻¹) and control treatment plots without sewage sludge application (CK, 0 t ha⁻¹). SS was applied to the soil surface of a Mongolian pine (Pinus sylvestris var. mongolica) plantation in Horqin Sandy Land, Inner Mongolia, China, to assess its potential effects on plants and soil. We analyzed tree growth performances (tree height, basal diameter, and diameter at breast height), understory traits (species diversity, coverage, and aboveground biomass), soil physical and chemical parameters (nutrient content, dissolved organic carbon, soil water content, bulk density, pH), and proxies of ecosystem services (soil organic carbon and total nitrogen stocks). The results showed that SS addition not only significantly increased soil nutrient contents, but also markedly enhanced aboveground productivity and plant coverage. Specifically, SS addition decreased soil bulk density and increased concentrations of soil organic carbon, total nitrogen, and total phosphorus and mineral nitrogen, and it also increased soil carbon and nitrogen stocks. Furthermore, the addition of SS significantly increased soil dissolved organic carbon contents and enhanced the fluorescence intensities of dissolved organic carbon components (humic acid-like and UV fulvic acid-like) in the topsoil (0–5 cm). This study provides evidence that SS is an acceptable, and possibly preferred organic fertilizer for improving the soil quality and tree–grass growth of Mongolian pine plantations.

Sudan III is a coloring agent used in chemical industries and food additives. This article uses spectroscopic and molecular docking methods to investigate the interaction of Sudan III with bovine serum albumin (BSA) under a physiological condition. Spectroscopic analysis of the emission quenching revealed that the quenching mechanism of BSA by Sudan III was static. The binding sites and constants of Sudan III–BSA complex were observed to be from 0.72 and 6.41 × 10² L·mol⁻¹ to 0.69 and 5.83 × 10² L·mol⁻¹ at 298 and 310 K, respectively. The enthalpy change (ΔH) and entropy change (ΔS) revealed that van der Waals forces and hydrogen bonds stabilized the Sudan III–BSA complex. Energy transfer from tryptophan to Sudan III occurred by a fluorescence resonance energy transfer mechanism, and the r distance (3.32 nm) had been determined. The results of UV–Vis absorption, synchronous, three-dimensional fluorescence, and circular dichroism spectra showed that Sudan III induced conformational changes of BSA. Molecular docking studies revealed that Sudan III situated within subdomain IIA of BSA. A study on the interaction between Sudan III and BSA was of fundamental importance for providing more information about the potential toxicological effect of chemicals at the molecular level.

This study investigates the interaction between tebuconazole and bovine serum albumin (BSA) in a physiological buffer (pH = 7.4) using the fluorescence quenching method to obtain the apparent binding constants (K) and number of binding sites (n) in the interaction between tebuconazole and BSA. The results revealed that tebuconazole can quench the intrinsic fluorescence of BSA through a static quenching procedure. It also shows that the thermodynamic parameters of enthalpy change (ΔH) and entropy change (ΔS) are negative, indicating that the interaction of tebuconazole with BSA is mainly driven by van der Waals forces and hydrogen bonds. The process of binding was a spontaneous process in which Gibbs free energy change was negative. The distance of r between the donor (BSA) and acceptor (tebuconazole) was calculated to be 0.68 nm based on Forster’s non-radiative energy transfer theory. Analysis of synchronous fluorescence, three-dimensional fluorescence and circular dichroism (CD) spectra demonstrates that tebuconazole can induce conformational changes of BSA.