TY - JOUR PB - MDPI SN - 20734344 Y1 - 2021/// VL - 11 JF - Catalysts A1 - Riaz, N. A1 - Fen, D.A.C.S. A1 - Khan, M.S. A1 - Naz, S. A1 - Sarwar, R. A1 - Farooq, U. A1 - Bustam, M.A. A1 - Batiha, G.E.-S. A1 - El Azab, I.H. A1 - Uddin, J. A1 - Khan, A. UR - https://www.scopus.com/inward/record.uri?eid=2-s2.0-85114950978&doi=10.3390%2fcatal11091112&partnerID=40&md5=7af21217d626bd252052247ec2576de7 AV - none TI - Iron-zinc co-doped titania nanocomposite: Photocatalytic and photobiocidal potential in combination with molecular docking studies ID - scholars14499 N2 - In the current research study, iron-zinc co-doped TiO2 was reported as an energy efficient material for the degradation of DIPA and inactivation of E. coli and S. aureus under visible light irradiation. In addition, molecular docking simulation was performed to provide further insight into possible targets for inhibiting bacterial development. The synthesized nanocomposites were screened and optimized for different synthesis and reaction parameters. The physicochemical properties of the synthesized nanocomposites were evaluated through different characterization techniques. The wet impregnation (WI) approach was among the most successful methods for the synthesis of Fe-Zn-TiO2 nanocomposite (NC) utilizing anatase titanium. Moreover, 66.5 (60 min reaction time) and 100 (190 min reaction time) chemical oxygen demand (COD) removal was obtained through optimized NC, i.e., 0.1Fe-0.4Zn metal composition and 300â?¦C calcination temperature. The energy consumption for the best NC was 457.40 KW h mâ??3. Moreover, 0.1Fe-0.4Zn-TiO2-300 was more efficient against S. aureus compared to E. coli with 100 reduction in 90 min of visible light irradiations. Furthermore, 0.1Fe-0.4Zn-TiO2-300 NC showed that the binding score for best docked conformation was â??5.72 kcal molâ??1 against β-lactamase from E. coli and â??3.46 kcal molâ??1 from S. aureus. The studies suggested the Fe-Zn in combination with TiO2 to be a possible inhibitor of β-lactamase that can be further tested in enzyme inhibition studies. © 2021 by the authors. Licensee MDPI, Basel, Switzerland. N1 - cited By 8 IS - 9 ER -