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Textile dyes and microbial contamination of surface water bodies have been recognized as emerging quality concerns around the globe. The simultaneous resolve of such impurities can pave the route for an amicable technological solution. This study reports the photocatalytic performance and the biocidal potential of nitrogen-doped TiO2 against reactive black 5 (RB5), a double azo dye and E. coli. Molecular docking was performed to identify and quantify the interactions of the TiO2 with β-lactamase enzyme and to predict the biocidal mechanism. The sol-gel technique was employed for the synthesis of different mol% nitrogen-doped TiO2. The synthesized photocatalysts were characterized using thermal gravimetric analysis (TGA), scanning electron microscopy (SEM), X-ray diffraction (XRD), Fourier transform infrared spectroscopy (FT-IR), Brunauer–Emmett–Teller (BET) and diffuse reflectance spectroscopy (DRS). The effects of different synthesis and reaction parameters were studied. RB5 dye degradation was monitored by tracking shifts in the absorption spectrum and percent chemical oxygen demand (COD) removal. The best nanomaterial depicted 5.57 nm crystallite size, 49.54 m2 g−1 specific surface area, 11–40 nm particle size with spherical morphologies, and uniform distribution. The RB5 decolorization data fits well with the pseudo-first-order kinetic model, and the maximum monolayer coverage capacity for the Langmuir adsorption model was found to be 40 mg g−1 with Kads of 0.113 mg−1. The LH model yielded a higher coefficient KC (1.15 mg L−1 h−1) compared to the adsorption constant KLH (0.3084 L mg−1). 90% COD removal was achieved in 60 min of irradiation, confirmed by the disappearance of spectral peaks. The best-optimized photocatalysts showed a noticeable biocidal potential against human pathogenic strain E. coli in 150 min. The biocidal mechanism of best-optimized photocatalyst was predicted by molecular docking simulation against E. coli β-lactamase enzyme. The docking score (−7.6 kcal mol−1) and the binding interaction with the active site residues (Lys315, Thr316, and Glu272) of β-lactamase further confirmed that inhibition of β-lactamase could be a most probable mechanism of biocidal activity. [ABSTRACT FROM AUTHOR]