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The unique hollow nanotube structure of 30% Co-CHNTs can efficiently degrade sulfamethoxazole antibiotics. [Display omitted] • The catalyst is synthesized by the impregnation-chemical reduction-calcination method. • The degradation rate of the catalyst to sulfamethoxazole within 30 min is 97.5%. • After the catalyst is calcined, the leaching of cobalt metal ions is reduced. • The catalyst still has a good degradation rate for sulfamethoxazole in natural water. • Non-radical singlet oxygen is the main active substance in the system. In this study, a new hollow nanotube material, 30% Co–CHNTs was prepared by the impregnation–chemical reduction–calcination method. This material can be used as a peroxymonosulfate (PMS) activator to catalyse the degradation of sulfamethoxazole (SMX). The best reaction conditions that correspond to the degradation rate of SMX, up to 97.5%, are as follows: the concentration of SMX is 10 mg L−1, the amount of catalyst is 0.20 g L−1, the dosage is 1.625 mM, and the solution pH is 6.00. X-ray photoelectron spectroscopy (XPS) and inductively coupled plasma optical emission spectrometry (ICP-OES) show that the calcined composites mainly stimulate an increase in the content of bivalent cobalt in PMS and reduce the leaching of cobalt ions after the reaction. Additionally, the 30% Co–CHNTs + PMS reaction system exhibits a reasonable SMX degradation rate in a natural organic matter solution and excellent stability after three repeated experiments. Furthermore, the possible degradation mechanism in the 30% Co–CHNTs + PMS reaction system was analysed through electron paramagnetic resonance (EPR) and free-radical capture experiments, and it was observed that the non-radical degradation of 1O 2 plays a leading role in SMX degradation. Finally, according to the nine degradation intermediates detected by liquid chromatography-mass spectrometry (LC–MS), four possible SMX degradation routes were proposed. This study proved that a 30% Co–CHNTs heterogeneous catalyst is easily prepared, inexpensive, and environmentally friendly and has potential application in antibiotic wastewater treatment. [ABSTRACT FROM AUTHOR]

Abstract The Brucella spp encounter stressful environment inside their host cells. The Lon protein is an important protease related to cellular protein degradation and resistance to stress in Brucella. However, the molecular mechanism between Lon protein and stress response was still unknown. In this study, it was found that the lon mutant exhibited obvious growth defect in TSB medium, compared with its parent strain. In addition, our results indicated that Lon protein was involved in resistance to various stress conditions and all the β-lactam antibiotics tested. Although deletion of this protease did not affect Brucella virulence in macrophage, the mutant strain was significantly attenuated in mice infection model at 1 week post infection, and the expression level of several cytokine genes was significantly changed in vivo. To gain insight into the genetic basis for the distinctive phenotypic properties exhibited by the lon mutant strain, RNA-seq was performed, and the result showed that various genes involved in stress response, quorum sensing and transcriptional regulation were significantly altered in Δ lon strain. Overall, these studies have preliminary uncovered the molecular mechanism between Lon protease, stress response and bacterial virulence. Highlights • The lon mutant exhibited obvious growth defect in TSB medium. • Lon protein was involved in resistance to various stress conditions and all the β-lactam antibiotics tested. • Genes involved in stress response, quorum sensing and transcriptional regulation were significantly altered in Δ lon strain. [ABSTRACT FROM AUTHOR]