Polycyclic aromatic hydrocarbons (PAHs) are widespread across the globe mainly due to long-term anthropogenic sources of pollution. The inherent properties of PAHs such as heterocyclic aromatic ring structures, hydrophobicity, and thermostability have made them recalcitrant and highly persistent in the environment. PAH pollutants have been determined to be highly toxic, mutagenic, carcinogenic, teratogenic, and immunotoxicogenic to various life forms. Therefore, this review discusses the primary sources of PAH emissions, exposure routes, and toxic effects on humans, in particular. This review briefly summarizes the physical and chemical PAH remediation approaches such as membrane filtration, soil washing, adsorption, electrokinetic, thermal, oxidation, and photocatalytic treatments. This review provides a detailed systematic compilation of the eco-friendly biological treatment solutions for remediation of PAHs such as microbial remediation approaches using bacteria, archaea, fungi, algae, and co-cultures. In situ and ex situ biological treatments such as land farming, biostimulation, bioaugmentation, phytoremediation, bioreactor, and vermiremediation approaches are discussed in detail, and a summary of the factors affecting and limiting PAH bioremediation is also discussed. An overview of emerging technologies employing multi-process combinatorial treatment approaches is given, and newer concepts on generation of value-added by-products during PAH remediation are highlighted in this review.

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Polycyclic Aromatic Hydrocarbons: Sources, Toxicity, and Remediation Approaches.

Comprehensive review of polycyclic aromatic hydrocarbons in water sources, their effects and treatments.

Biomimetic dynamic membrane for aquatic dye removal.

Nanofiltration plays an increasingly large role in many industrial applications, such as water treatment (e.g., desalination, water softening, and fluoride removal) and resource recovery (e.g., alk...

Sharpening Nanofiltration: Strategies for Enhanced Membrane Selectivity.

Nanozymes, defined as nanomaterials with enzyme-like activity, have attracted extensive interest in both fundamental and applied research. Laccases are members of the multi-copper oxidases, which are utilized as green catalysts in the environmental catalysis and biochemical industry. In this paper, we report a facile strategy for the preparation of a new class of nanozyme (denoted as CH-Cu) with laccase-like activity inspired by the structure of the active site and the electron transfer pathway of laccase via the coordination of Cu+/Cu2+ with a cysteine (Cys)-histidine (His) dipeptide. The CH-Cu nanozymes exhibit excellent catalytic activity, recyclability and substrate universality and have a similar Km (Michaelis constant) and a higher vmax (maximum rate) than laccase at the same mass concentration. They are robust under a variety of conditions, such as extreme pH, high temperature, long-term storage and high salinity, which can cause severe loss in the catalytic activity of laccase. Higher efficacy of the CH-Cu nanozymes compared with laccase in the degradation of chlorophenols and bisphenols is also demonstrated in a batch reaction. Furthermore, a method for the quantitative detection of epinephrine by a smart phone is established based on the CH-Cu nanozymes. We believe that this nanozyme has promising applications in environmental catalysis and rapid detection and expect that combining key peptides as metal ligands with metal ions to mimic the structure of the catalytic center of a natural enzyme will be a general and important strategy for the design and synthesis of a new type of nanozyme that can be used in various applications.

Construction of a bioinspired laccase-mimicking nanozyme for the degradation and detection of phenolic pollutants

Removal of polycyclic aromatic hydrocarbons by nanofiltration membranes: Rejection and fouling mechanisms

Application of biocatalytic membrane is promising in food, pharmaceutical, and water treatment industries, whereas enzyme immobilization is the key step of biocatalytic membrane preparation Thus, how to minimize the negative effect of immobilization on enzyme performance is required to answer In this work, we proposed a platform for biocatalytic membrane preparation and immobilization mechanism investigation based on polydopamine (PDA) coating, which was demonstrated by immobilizing five commonly used enzymes (laccase, glucose oxidase, lipase, pepsin, and dextranase) on three commercially available membranes via three immobilization mechanisms (electrostatic attraction, covalent bonding, and hydrophobic adsorption), respectively By examining the enzyme loading, activity, and kinetics under different immobilization mechanisms, we found that except for dextranase, enzyme immobilization via electrostatic attraction retained the most activity, whereas covalent bonding and hydrophobic adsorption were detrimental to enzyme conformation Enzyme immobilization via covalent bonding ensured a high enzyme loading, and hydrophobic adsorption was only suitable for lipase and dextranase immobilization Moreover, the properties of functional groups around the enzyme active center should be considered for the selection of suitable immobilization strategy (ie, avoid covering the active center by membrane carrier) This work not only established a versatile platform for biocatalytic membrane preparation but also provided a novel methodology to evaluate the effect of immobilization mechanisms on enzyme performance

Biocatalytic Membrane Based on Polydopamine Coating: A Platform for Studying Immobilization Mechanisms

Regenerable biocatalytic nanofiltration membrane for aquatic micropollutants removal

Aflatoxin B1 removal by multifunctional membrane based on polydopamine intermediate layer

Can graphene oxide improve the performance of biocatalytic membrane

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