A new study published in Frontiers in Bioengineering and Biotechnology by Xuanyu Chen, Prithvendra Singh, Kaiwei Luo, Qianwei Ma, and Ningjun Jiang of Southeast University’s Institute of Geotechnical Engineering, working with the Jiangsu Key Laboratory of Low Carbon and Sustainable Geotechnical Engineering and the Indian Institute of Technology Bombay, has now demonstrated that laccase-based enzymatic pretreatment produces strikingly different engineering responses depending on whether the humic-rich soil is being solidified or dewatered. The research team used an artificial humic-rich soil containing 10 percent humic acid, classified as organic clay under the Unified Soil Classification System, to compare laccase pretreatment in composite-binder solidification and slurry dewatering. The artificial soil was prepared from 18 percent quartz-rich silt, 27 percent kaolin, 45 percent calcium bentonite, and 10 percent commercial humic acid, providing a reproducible humic-rich model system for comparing the tested treatment routes.

Laccase is well suited to modifying organic interfaces because it oxidizes a broad range of phenolic and aromatic substrates under mild aqueous conditions using molecular oxygen as the terminal electron acceptor. Its effective reaction domain can be extended with a low-molecular-mass redox mediator such as 2,2′-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid), commonly abbreviated ABTS, which transfers oxidative equivalents from the enzyme to less accessible substrates. For humic-rich soil, however, a larger reaction domain cannot be assumed to be universally beneficial. Humic substances themselves participate in laccase-driven transformations and can also aggregate with or inhibit laccase, so enzyme performance depends on the physicochemical environment in which the catalytic system operates. The engineering question is therefore not whether ABTS increases laccase reactivity in isolation, but whether the resulting spatial pattern of organic transformation is favorable for the subsequent engineering process.

The experimental program comprised four parts: a laccase-dose comparison for solidification, a component-comparison test of laccase alone, laccase plus ABTS, and laccase plus ABTS plus carboxymethyl chitosan, bench-scale coagulation and flocculation with vacuum filtration, and geotextile-tube dewatering. For solidification, the treated soil was mixed with 8 percent of a self-developed calcium-rich composite curing agent consisting of carbide residue, gypsum, and Portland cement at a dry-mass ratio of 20:1:1 after 24 hours of pretreatment. For dewatering, the same solids were dispersed as a high-water-content slurry with an initial water content of 383.9 percent on a dry-mass basis and conditioned with polyaluminum chloride followed by carboxymethyl chitosan or cationic polyacrylamide.

The solidification results were unambiguous. At laccase dosages of 20,000 and 40,000 units per kilogram of dry soil, the 14-day unconfined compressive strength reached 841.4 and 818.3 kilopascals respectively, compared with only 434.9 kilopascals for the untreated control. The 20,000-unit dosage was therefore selected for subsequent experiments because increasing the nominal laccase input to 40,000 units per kilogram did not provide additional strength improvement. In the component-comparison test, the 14-day strength was 797.4 kilopascals with laccase alone, 630.6 kilopascals with laccase plus ABTS, 518.0 kilopascals with laccase plus ABTS plus carboxymethyl chitosan, and 410.6 kilopascals for the control. Laccase alone combined the highest 14-day strength with the lowest axial expansion of 1.74 percent, compared with 2.58 percent for the control. The addition of ABTS, and particularly the subsequent incorporation of carboxymethyl chitosan, progressively diminished the strengthening effect rather than providing an additive benefit.

Microstructural evidence from the solidification branch supported this interpretation. Scanning electron microscopy showed that the 14-day laccase-treated specimen had the densest interparticle morphology, with particle surfaces more extensively covered by cementitious products and adjacent particles connected by more continuous solid bridges. Energy-dispersive X-ray spectroscopy revealed that the calcium content increased from 9.63 weight percent in the control to 13.65 weight percent in the laccase-treated specimen, with the atomic calcium-to-silicon ratio rising from 0.410 to 0.774. X-ray diffraction patterns showed broadly similar crystalline-phase assemblages dominated by quartz, calcite, and portlandite, indicating that enzymatic pretreatment did not alter the principal aluminosilicate mineral framework but instead produced treatment-dependent differences in the relative prominence of existing calcium-bearing reflections.

In contrast, mediator addition benefited slurry treatment. In the bench-scale tests, laccase plus ABTS followed by polyaluminum chloride and carboxymethyl chitosan reduced supernatant turbidity to 3.73 nephelometric turbidity units, the lowest value among the chitosan-based formulations, and reduced vacuum-filtrate turbidity to 81.7 units while decreasing cake water content to 57.66 percent. Notably, two formulations with similar zeta potentials of approximately -7 millivolts showed markedly different turbidity and cake water content, indicating that charge reduction alone did not determine clarification performance. Once electrostatic repulsion is reduced, aggregate architecture, floc strength, compressibility, and pore connectivity become increasingly important in controlling dewaterability.

The difference between formulations became even more pronounced during geotextile-tube drainage. Although polyaluminum chloride plus cationic polyacrylamide produced the fastest initial release of water, releasing 725 milliliters within the first 5 minutes, the laccase plus ABTS plus polyaluminum chloride plus carboxymethyl chitosan route subsequently achieved the greatest cumulative water release. At 30 hours, the cumulative filtrate volume reached 1,702.8 milliliters for the enzymatic route, compared with 1,340 milliliters for polyaluminum chloride plus carboxymethyl chitosan and 1,392 milliliters for polyaluminum chloride plus cationic polyacrylamide, representing increases of 27.1 percent and 22.3 percent respectively. The final central-region cake water content was 84.94 percent for the enzymatic route, substantially lower than 112.19 percent for the chitosan route and 127.23 percent for the polyacrylamide route. The directly collected filtrate from the enzymatic route also remained relatively clear at 9.99 turbidity units, compared with 82.86 units for the chitosan route without biochemical pretreatment.

Dissolved organic carbon analysis revealed a paradoxical finding. The DOC concentration decreased from 40.50 milligrams of carbon per liter in untreated soil to 29.07 after laccase treatment, a reduction of 28.2 percent, and further decreased to 20.33 milligrams of carbon per liter after ABTS addition, representing a reduction of 49.8 percent relative to untreated soil. Yet the corresponding 14-day strength decreased from 797.4 to 630.6 kilopascals. Thus, maximizing the reduction in extractable dissolved organic carbon was not equivalent to maximizing solidification performance. The authors suggest that differences in the location or form of organic-matter transformation influenced subsequent particle-binder interactions, with laccase alone producing a more favorable interfacial condition for cementation while ABTS-assisted treatment extended organic transformation over a broader fraction of the system.

The contrasting effects of ABTS on solidification and dewatering reflect the different structural requirements of the two engineering processes. In composite-binder solidification, performance depends on the development of mechanically effective particle-binder contacts during curing, whereas slurry dewatering depends on aggregate formation and the persistence of water-conducting pathways during filtration and cake consolidation. In compacted soil, strength develops primarily at particle-binder contacts; in slurry, organic matter and mineral particles are dispersed throughout the aqueous phase, providing conditions for ABTS-mediated electron transfer to extend organic modification beyond the immediate enzyme-accessible region. ABTS therefore had opposite engineering effects in the two processes: it reduced solidification performance relative to laccase alone but enhanced prolonged chitosan-based slurry dewatering. The authors conclude that the enzyme-mediator combination should be selected according to the intended engineering process rather than treated as universally additive, and they note that validation with natural humic-rich soils and sediments will further define the range of applicability of these formulation trends.

Subject of Research: Enzymatic soil pretreatment with laccase and ABTS shows opposite effects on solidification and dewatering of humic-rich soil

Article Title: Differential effects of ABTS-assisted laccase pretreatment on solidification and dewatering of humic-rich soil

Article References: Chen, X., Singh, P., Luo, K., Ma, Q., & Jiang, N. (2026). Differential effects of ABTS-assisted laccase pretreatment on solidification and dewatering of humic-rich soil. Frontiers in Bioengineering and Biotechnology, 14, Article 1996007. https://doi.org/10.3389/fbioe.2026.1996007

Image Credits: AI Generated

DOI: 10.3389/fbioe.2026.1996007

Keywords: laccase, ABTS, humic-rich soil, soil solidification, slurry dewatering, redox mediator, geotextile tube, unconfined compressive strength, calcium carbide residue, dissolved organic carbon, enzymatic pretreatment, biogeotechnics

The central challenge the team addressed is a familiar one in analytical electrochemistry. Thiocyanate and sulfide ions are both difficult to oxidize directly at electrode surfaces, because the heterogeneous electron transfer between the electrode and these anions is intrinsically slow and often accompanied by fouling of the surface by oxidation products such as elemental sulfur. Direct anodic oxidation of sulfide, for example, has long been known to deposit sulfur films on electrodes, degrading their performance over time. Mediated electrocatalysis offers an elegant workaround: instead of forcing the analyte to surrender electrons directly to the solid electrode, a dissolved redox-active mediator is first oxidized at the electrode and then chemically oxidizes the analyte in solution, regenerating the reduced form of the mediator and completing a catalytic cycle. In electrochemical notation this is the classic EC′ mechanism, where an electrode reaction (E) is followed by a homogeneous chemical reaction (C′) that consumes the electrogenerated species.

Chlorpromazine is exceptionally well suited to this role. The phenothiazine core undergoes a well-defined, reversible one-electron oxidation in aqueous media, converting the parent compound into a stable radical cation that is a potent chemical oxidant. Because the redox couple sits at a potential that is accessible on many electrode materials, the oxidized form can be generated cleanly and reproducibly. The Iranian team chose boron-doped diamond as the working electrode, a material prized in electrochemistry for its extraordinary chemical inertness, wide potential window in water, and resistance to fouling. These properties make BDD an ideal substrate for studying mediated oxidation reactions without the complicating background chemistry that plagues more reactive carbon or metal surfaces. Using cyclic voltammetry, the researchers first characterized the redox behavior of chlorpromazine itself in aqueous buffer, establishing the standard potential and the kinetic parameters that govern the electron transfer at the diamond surface.

The crucial methodological innovation of the study lies in its use of digital simulation software, specifically DigiSim 3, to fit simulated cyclic voltammograms to the experimental curves. Digital simulation works by numerically solving the coupled partial differential equations that describe mass transport, electron transfer, and homogeneous chemical kinetics in the diffusion layer adjacent to the electrode. The researcher proposes a mechanism, assigns plausible values for the diffusion coefficients, heterogeneous electron-transfer rate constants, charge-transfer coefficients, and catalytic rate constants, and the software generates a predicted voltammogram. By iteratively adjusting these parameters until the simulated curve overlays the experimental data, the team could extract quantitative kinetic information that would be nearly impossible to obtain from peak currents and peak potentials alone. The quality of the fit then becomes a stringent test of the proposed mechanism: if the assumed reaction scheme is wrong, no reasonable parameter set will reproduce the observed peak shapes, positions, and scan-rate dependence.

When thiocyanate was added to the solution containing chlorpromazine, the cyclic voltammograms changed in a manner diagnostic of electrocatalysis. The anodic peak current for the oxidation of the mediator increased substantially, while the corresponding cathodic peak on the reverse scan diminished, exactly the signature expected when the electrochemically generated oxidized chlorpromazine is consumed by a fast chemical reaction with thiocyanate in the diffusion layer. The same behavior appeared with sulfide. The team systematically varied the analyte concentration and the potential scan rate, mapping out how the catalytic response evolved across both dimensions. At slow scan rates, the chemical step has more time to consume the oxidized mediator, amplifying the catalytic enhancement; at fast scan rates, the voltammetry increasingly reflects the intrinsic kinetics of the mediator redox couple itself. This scan-rate dependence, combined with concentration dependence, provided the experimental scaffolding on which the digital simulations were built.

The fitted parameters tell a quantitative story. The diffusion coefficient of thiocyanate was determined to be (2.08 ± 0.05) × 10⁻⁵ cm² s⁻¹, while sulfide diffused somewhat faster at (5.08 ± 0.16) × 10⁻⁵ cm² s⁻¹, consistent with the smaller hydrodynamic radius of the hydrated sulfide species. The heterogeneous electron-transfer rate constant for the chlorpromazine couple on boron-doped diamond came out at 0.0066 cm s⁻¹ for both analyte systems, indicating a moderately fast but not diffusion-limited surface reaction. The charge-transfer coefficients, which describe the symmetry of the energy barrier for electron transfer, were 0.605 ± 0.037 for the thiocyanate system and 0.550 ± 0.025 for sulfide, values close to the idealized 0.5 that characterizes a well-behaved outer-sphere electron transfer. Most strikingly, the catalytic rate constants, which quantify how rapidly the oxidized mediator attacks the analyte in solution, reached (4.05 ± 0.42) × 10⁴ M⁻¹ s⁻¹ for thiocyanate and (5.34 ± 1.92) × 10⁴ M⁻¹ s⁻¹ for sulfide, confirming that the homogeneous chemical steps are genuinely fast and efficient.

The satisfactory agreement between simulated and experimental voltammograms across the full range of conditions gives the authors confidence that the EC′ mechanism they propose is the correct description of the chemistry. In other words, the oxidized chlorpromazine radical cation formed at the diamond surface diffuses into the solution, transfers oxygen-equivalent oxidizing power to thiocyanate or sulfide, and is reduced back to its parent form, ready to be re-oxidized at the electrode. This catalytic turnover is what produces the amplified anodic currents that underpin potential analytical applications. The study builds on the group’s earlier work, including a 2017 investigation of chlorpromazine-mediated oxidation of arsenic(III) and iron(II) and a 2024 study that revealed more complex EEC and EC′EC mechanisms when the mediator operates in the presence of the amino acid L-cysteine. Together, these papers sketch a versatile mediator chemistry whose mechanism shifts depending on the identity and reactivity of the target analyte.

Why does this matter beyond the electrochemistry community? Thiocyanate is a clinically and forensically significant biomarker. It is the principal metabolite of cyanide exposure, and elevated salivary thiocyanate levels are associated with tobacco smoking, making it a target for noninvasive screening methods ranging from ion-selective electrodes to colorimetric assays. Sulfide, meanwhile, occupies a dual identity: hydrogen sulfide is a notorious toxic gas and an environmental pollutant in wastewater and food spoilage, yet it is also increasingly recognized as a biologically produced signaling molecule, or gasotransmitter, whose concentration in living cells is actively regulated. Analytical methods for sulfide therefore span environmental monitoring, food safety, and biomedical research, employing everything from nanoporous gold electrodes to fluorescent probes and smartphone-based colorimetry. A robust, mechanistically understood electrocatalytic route to oxidizing both species could feed into the design of simpler, cheaper electrochemical sensors that do not suffer from the fouling problems of direct oxidation.

The study also contributes to a broader renaissance of interest in the electrochemistry of phenothiazines. Recent work has mapped the surprisingly complex three-electron oxidation pathway of chlorpromazine, and other groups have developed nanostructured electrodes, from nickel phosphate to antimony vanadate nanospheres, for detecting the drug itself in biological samples. The Ionics paper inverts that perspective: rather than detecting chlorpromazine, it deploys the drug as an active catalytic agent. The combination of a fouling-resistant diamond electrode, a cheap and commercially available mediator, and the mechanistic rigor of digital simulation offers a template for how mediated electrocatalysis can be characterized quantitatively rather than merely demonstrated. As sensor developers seek mediators whose kinetics are fully understood and whose behavior can be predicted computationally, this fusion of experiment and simulation may prove to be the study’s most lasting contribution, turning a vintage antipsychotic into a precision tool for environmental and analytical chemistry.

Subject of Research: Electrocatalytic oxidation mechanisms of thiocyanate and sulfide mediated by chlorpromazine at boron-doped diamond electrodes, characterized by digital electrochemical simulation

Article Title: A comprehensive experimental and theoretical elucidation of the electrocatalytic oxidation mechanisms of thiocyanate and sulfide mediated by chlorpromazine: supported by digital electrochemical simulations

Article References: Salimi, A., Amini, N., & Naderi, K. (2026). A comprehensive experimental and theoretical elucidation of the electrocatalytic oxidation mechanisms of thiocyanate and sulfide mediated by chlorpromazine: supported by digital electrochemical simulations. Ionics. https://doi.org/10.1007/s11581-026-07571-3

Image Credits: AI Generated

DOI: 10.1007/s11581-026-07571-3

Keywords: chlorpromazine, thiocyanate, sulfide, electrocatalysis, boron-doped diamond electrode, cyclic voltammetry, digital simulation, EC′ mechanism, reaction kinetics, phenothiazine, electrochemical sensing, redox mediator

The research team, led by Khadega A. Al-Maqdi of UAE University together with colleagues at Khalifa University, the University of Arkansas at Little Rock, and collaborators, chose horseradish peroxidase (HRP) for good reason. Peroxidases are oxidoreductase enzymes that use hydrogen peroxide to oxidize a broad range of substrates, and HRP in particular has long attracted attention for water remediation because of its high catalytic efficiency and selectivity. The catch is operational: free enzymes in solution are fragile, difficult to recover, and quickly lose activity under the temperature swings, pH extremes, and oxidative conditions of real treatment scenarios. Poor reusability drives up cost and has largely confined enzyme-based remediation to the laboratory. Immobilization on a solid support is the standard remedy, and the nature of that support can make or break the technology.

The support selected here was UiO-66-NH2, a zirconium-based metal–organic framework (MOF) built from zirconium chloride and 2-aminoterephthalic acid. MOFs are crystalline, highly porous materials in which metal ions or clusters are coordinated to organic linkers, producing enormous internal surface areas and tunable pore architectures. UiO-66-NH2 brings additional advantages: the strong zirconium–oxygen coordination bonds confer exceptional structural and aqueous stability, while pendant amino groups on the linkers promote hydrogen bonding and electrostatic interactions at the enzyme–MOF interface, helping the protein adhere and remain stable. Immobilization was deliberately simple and gentle. Five milligrams of the MOF were dispersed in solutions of HRP at concentrations ranging from 0.5 to 4 milligrams per milliliter, shaken for four hours, and then collected by centrifugation and washed to remove unbound enzyme. This physical adsorption approach preserves the enzyme’s native structure better than covalent coupling or crosslinking, at the cost of a need to verify that the protein does not leach away.

Optimization experiments showed that relative activity rose as the HRP loading concentration increased from 0.5 to 1 milligram per milliliter but plateaued beyond that point, indicating that the MOF had reached its maximum uptake capacity at 1 milligram per milliliter, which was used for all subsequent work. Leaching tests addressed the Achilles heel of physical immobilization: after the first wash, minimal enzyme was detected in the wash solution, and after the second wash no unbound HRP appeared in the supernatant at all, confirming that the enzyme was effectively anchored. The composite was then subjected to a battery of characterization techniques. Scanning electron microscopy revealed that the MOF crystallized as ball-shaped particles whose morphology was unchanged by enzyme loading, while energy-dispersive X-ray spectroscopy detected increases in the carbon, nitrogen, and oxygen signals after immobilization, consistent with protein incorporation. Powder X-ray diffraction showed that the characteristic diffraction peaks of the framework survived intact, and thermogravimetric analysis revealed an additional low-temperature weight loss in the composite attributable to protein decomposition, further evidence of successful binding.

Brunauer–Emmett–Teller surface area measurements added a telling detail. The bare MOF had a surface area of 256.27 square meters per gram, which dropped to 207.33 square meters per gram after enzyme loading, with pore volume falling from 0.17 to 0.14 cubic centimeters per gram. Both materials displayed Type I nitrogen adsorption isotherms, indicating predominantly microporous character. The reduction suggests that HRP molecules partially blocked the framework’s pores, a pattern seen repeatedly in other enzyme–MOF systems such as laccase on MIL-53(Al) and beta-lactamase on ZIF-8. Fourier-transform infrared spectroscopy told a complementary story: the amide I and amide II bands characteristic of the protein’s peptide bonds overlapped with the framework’s own absorptions in the 1500 to 1700 per centimeter region, producing broadened signals without shifts or signs of framework degradation. Together the data confirmed that immobilization neither destroyed the MOF’s crystallinity nor its thermal stability, which persisted up to roughly 350 to 400 degrees Celsius.

Functional testing revealed that immobilization did more than just fix the enzyme in place; it changed its operating envelope. Both free and immobilized HRP performed best at pH 4, with a narrow operational window from pH 3 to 5, but the immobilized enzyme showed roughly 30 percent higher activity than the free enzyme at pH 3, hinting at improved stability or substrate accessibility under acidic conditions. More striking was the temperature shift: free HRP peaked at 30 degrees Celsius, while HRP@UiO-66-NH2 reached maximum activity at 40 degrees and outperformed the free enzyme by around 10 percent or more at 50 and 70 degrees. The peroxide story was equally significant. Free HRP achieved maximum activity at about 0.72 millimolar hydrogen peroxide and then declined sharply, because excess peroxide drives the enzyme’s heme into irreversibly inactive species. The immobilized enzyme peaked at 1.08 millimolar and retained substantial activity at 1.62 and 2.43 millimolar, indicating that the framework shields the protein from oxidative damage and restricts the conformational changes that lead to heme destruction.

Reusability, the economic linchpin of any immobilized enzyme, proved robust. Over four consecutive reaction cycles, HRP@UiO-66-NH2 retained approximately 95 percent of its initial activity, with a decline to around 60 percent only in the fifth cycle, likely from leaching or denaturation. The authors are careful to note, however, that post-use characterization was not performed, so retained catalytic activity demonstrates functional reusability but does not directly prove that the framework’s crystallinity and morphology survived the cycles; future work combining post-cycle diffraction, spectroscopy, microscopy, and leaching measurements is needed to distinguish enzyme deactivation, mass-transfer limitations, and possible structural changes in the MOF.

The real test came with pollutants. The team challenged the biocatalyst with a mixture of nine structurally diverse emerging pollutants detected in water sources across China, the United Arab Emirates, Poland, and Brazil: 2-mercaptobenzothiazole (a rubber-industry chemical), paracetamol, the antibiotic sulfamethoxazole, the preservative methylparaben, salicylic acid, the antibiotic lincomycin hydrochloride, the beta-blocker atenolol, the fungicide thiabendazole, and the insect repellent DEET. Degradation was quantified by liquid chromatography–tandem mass spectrometry in multiple-reaction-monitoring mode, a sensitive approach that tracks the disappearance of each compound’s characteristic molecular transitions. Within 30 minutes, HRP@UiO-66-NH2 degraded 99.7 percent of 2-mercaptobenzothiazole and 97.4 percent of paracetamol, while the remaining pollutants were removed far less efficiently, a pattern consistent with earlier reports that certain peroxidases struggle with specific substrates, possibly because of competition or inhibition within the mixture rather than inherent inability.

That gap is where redox mediators enter the picture. The team added 1-hydroxybenzotriazole (HOBT), a small molecule that HRP oxidizes to a reactive species capable of transferring oxidative equivalents to pollutants that interact poorly with the enzyme’s active site. The effect was dramatic and pollutant-dependent. Degradation of sulfamethoxazole rose from 23.3 to 53.1 percent, methylparaben from 14.5 to 57.6 percent, and salicylic acid from 12.4 to 54.3 percent, while MBT and paracetamol, already nearly eliminated, showed no further change, and thiabendazole, lincomycin, and atenolol remained largely untouched. Comparisons with free HRP added nuance: free enzyme plus HOBT pushed sulfamethoxazole degradation to 80.2 percent, roughly 30 percentage points higher than the immobilized version, possibly because minor conformational changes imposed by the support alter substrate selectivity. Yet the immobilized enzyme outperformed free HRP on DEET by more than 10 percent, encouraging for a notoriously recalcitrant compound. Unlike MOF-based adsorption, which merely accumulates pollutants on finite surface sites and requires regeneration, the enzyme–MOF composite catalytically transforms susceptible molecules through repeated oxidation cycles powered by hydrogen peroxide.

The authors are candid about limitations. The experiments were conducted in a controlled buffered model-water system, so performance may differ in real wastewater laden with organic matter, dissolved ions, and competing contaminants. Removal of a parent compound does not confirm complete mineralization or reduced toxicity, and transformation products were not identified, meaning the proposed mediator-assisted mechanisms remain plausible rather than proven pathways. Still, the study demonstrates that a zirconium MOF can simultaneously protect a fragile enzyme, extend its thermal and peroxide tolerance, enable four-cycle reuse, and, with a selectively applied redox mediator, broaden its reach across chemically diverse micropollutants. The researchers propose evaluating HRP@UiO-66-NH2 as a targeted polishing treatment for emerging pollutants, with mediators deployed according to pollutant-specific effects, and call for follow-up work on transformation products, toxicity before and after treatment, real-matrix performance, and scalability. If those hurdles are cleared, enzyme–MOF composites of this kind could move from the laboratory bench toward a genuine role in safeguarding drinking water.

Subject of Research: Immobilization of horseradish peroxidase on the metal–organic framework UiO-66-NH2 for enzymatic degradation of emerging water pollutants

Article Title: Efficient enzyme-mediated degradation of various emerging pollutants, including 2-mercaptobenzothiazole, paracetamol, and sulfamethoxazole, using HRP@UiO-66-NH2

Article References: Al-Maqdi, K. A., Alneyadi, S., Elmerhi, N., Siddig, L. A., Alzamly, A., Shah, I., & Ashraf, S. S. (2026). Efficient enzyme-mediated degradation of various emerging pollutants, including 2-mercaptobenzothiazole, paracetamol, and sulfamethoxazole, using HRP@UiO-66-NH2. Environmental Science and Pollution Research. https://doi.org/10.1007/s11356-026-38269-8

Image Credits: AI Generated

DOI: 10.1007/s11356-026-38269-8

Keywords: horseradish peroxidase, UiO-66-NH2, metal–organic framework, enzyme immobilization, emerging pollutants, water remediation, bioremediation, redox mediator, HOBT, sulfamethoxazole, paracetamol, LC–MS/MS