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Bioremediation is a promising technology that can eliminate the drawbacks of conventional treatment methods in removing harmful toxic metals including chromium(VI). Therefore, in this study, fungal hyphae modified with graphite and reduced graphene oxide were synthesized and assessed for their potential to bioremediate heavy metals for the first time in the literature. The effects of the carbon-based materials on microbial structure were characterized using scanning electron microscopy analysis. Thermogravimetric, RAMAN, X-ray diffraction, and enzymatic analyzes were performed to determine the role of functional groups. In addition, batch adsorption experiments utilizing response surface methodology were conducted to optimize operating parameters such as time (1-11 h), chromium (10-50 mg/L), and graphite/reduced graphene oxide (0.1-1 g/L). The maximum adsorption capacity with the graphene fungal hyphae was determined to be 568 mg.g -1 , which is 9.7 times that of the crude fungal hyphae. The Cr(VI) removal for fungal hyphae-graphite and fungal hyphae-reduced graphene oxide biocomposites was 98.25% and 98.49%, respectively. The isothermal and kinetic results perfectly matched the 2nd order pseudo-model and Langmuir model in terms of the nature of the adsorption process. The laboratory scale test results indicate that fungal hyphae modified with graphite and reduced graphene oxide have a high adsorption capacity, suitable for the removal of chromium (VI) from wastewater.

Laccases or laccase-like multicopper oxidases have great potential in bioremediation to oxidase phenolic or non-phenolic substrates. However, their inability to maintain stability in harsh environmental conditions and against non-substrate compounds is one of the main reasons for their limited use. The gene (mco) encoding multicopper oxidase from Bacillus mojavensis TH309 were cloned into pET14b( +), expressed in Escherichia coli, and purified as histidine tagged enzyme (BmLMCO). The molecular weight of the enzyme was about 60 kDa. The enzyme exhibited laccase-like activity toward 2,6-dimethoxyphenol (2,6-DMP), syringaldazine (SGZ), and 2,2'-azino-bis (3-ethylbenzothiazoline-6-sulphonic acid) (ABTS). The highest enzyme activity was recorded at 80 °C and pH 8. BmLMCO showed a half-life of ~ 305, 99, 50, 46, 36, and 20 min at 40, 50, 60, 70, 80, and 90 °C, respectively. It retained more than 60% of its activity after pre-incubation in the range of pH 5-12 for 60 min. The enzyme activity significantly increased in the presence of 1 mM of Cu 2+ . Moreover, BmLMCO tolerated various chemicals and showed excellent compatibility with organic solvents. The Michaelis constant (K m ) and the maximum velocity (V max ) values of BmLMCO were 0.98 mM and 93.45 µmol/min, respectively, with 2,6-DMP as the substrate. BmLMCO reduced the antibacterial activity of cefprozil, gentamycin, and erythromycin by 72.3 ± 1.5%, 79.6 ± 6.4%, and 19.7 ± 4.1%, respectively. This is the first revealing shows the recombinant production of laccase-like multicopper oxidase from any B. mojavensis strains, its biochemical properties, and potential for use in bioremediation., (© 2023. The Author(s), under exclusive licence to Springer-Verlag GmbH Germany, part of Springer Nature.)