Characteristics, mechanisms and bacteria behavior of photocatalysis with a solid Z-scheme Ag/AgBr/g-C3N4 nanosheet in water disinfection

Fig. Transfer mechanism of photogenerated charge carriers in the Ag/AgBr/CNNS photocatalyst. [Display omitted] •Ag/AgBr/CNNS exhibited efficient bactericidal ability at a low light intensity.•The transfer mechanisms in the photocatalyst were analyzed and proved.•The subcellular mechanism of E. coli...

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Published inApplied catalysis. A, General Vol. 590; p. 117282
Main Authors Yan, Yichang, Zhou, Xiaoqin, Yu, Peng, Li, Zifu, Zheng, Tianlong
Format Journal Article
LanguageEnglish
Published Amsterdam Elsevier B.V 25.01.2020
Elsevier Science SA
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Summary:Fig. Transfer mechanism of photogenerated charge carriers in the Ag/AgBr/CNNS photocatalyst. [Display omitted] •Ag/AgBr/CNNS exhibited efficient bactericidal ability at a low light intensity.•The transfer mechanisms in the photocatalyst were analyzed and proved.•The subcellular mechanism of E. coli during the disinfection was studied. In this study, a series of Ag/AgBr/g-C3N4 nanosheet (CNNS) photocatalysts were prepared by a more environmental-friendly method. The prepared material was characterized and then applied in photocatalytic disinfection of Escherichia coli (E. coli) under mild visible light for the first time. Results showed that all E. coli (108 CFU/mL) could be eliminated under irradiation at 20 mW·cm−2 within 120 min. Based on the energy band determination and electron spin resonance analysis, the Z-scheme in the photocatalyst was responsible for the enhanced disinfection effects where Ag nanoparticles acting as the electron mediator. Scavenger experiments demonstrated that photogenerated holes and superoxide radicals were the main reactive species. The variations in cell membrane permeability, cell membrane structure, enzyme activities and ATP concentration were monitored, and results indicated that the reactive species overwhelmed the bacterial defense mechanism, leading to the penetration of bacterial membranes, release of ions, protein fragmentation, and eventually, inactivation.
ISSN:0926-860X
1873-3875
DOI:10.1016/j.apcata.2019.117282