The green synthesis (GS) of different metallic nanoparticles (MNPs) has re-evaluated plants, animals and microorganisms for their natural potential to reduce metallic ions into neutral atoms at no expense of toxic and hazardous chemicals. Contrary to chemically synthesized MNPs, GS offers advantages of enhanced biocompatibility and thus has better scope for biomedical applications. Plant, animals and microorganisms belonging to lower and higher taxonomic groups have been experimented for GS of MNPs, such as gold (Au), silver (Ag), copper oxide (CuO), zinc oxide (ZnO), iron (Fe 2 O 3 ), palladium (Pd), platinum (Pt), nickel oxide (NiO) and magnesium oxide (MgO). Among the different plant groups used for GS, angiosperms and algae have been explored the most with great success. GS with animal-derived biomaterials, such as chitin, silk (sericin, fibroin and spider silk) or cell extract of invertebrates have also been reported. Gram positive and gram negative bacteria, different fungal species and virus particles have also shown their abilities in the reduction of metal ions. However, not a thumb rule, most of the reducing agents sourced from living world also act as capping agents and render MNPs less toxic or more biocompatible. The most unexplored area so far in GS is the mechanism studies for different natural reducing agents expect for few of them, such as tea and neem plants. This review encompasses the recent advances in the GS of MNPs using plants, animals and microorganisms and analyzes the key points and further discusses the pros and cons of GS in respect of chemical synthesis.

Due to recalcitrance of some pharmaceutically active compounds (PhACs), conventional wastewater treatment is not able to remove them effectively. Therefore, their occurrence in surface water and potential environmental impact has raised serious global concern. Biological transformation of these contaminants using white-rot fungi (WRF) and their oxidoreductase enzymes has been proposed as a low cost and environmentally friendly solution for water treatment. The removal performance of PhACs by a fungal culture is dependent on several factors, such as fungal species, the secreted enzymes, molecular structure of target compounds, culture medium composition, etc. In recent 20 years, numerous researchers tried to elucidate the removal mechanisms and the effects of important operational parameters such as temperature and pH on the enzymatic treatment of PhACs. This review summarizes and analyzes the studies performed on PhACs removal from spiked pure water and real wastewaters using oxidoreductase enzymes and the data related to degradation efficiencies of the most studied compounds. The review also offers an insight into enzymes immobilization, fungal reactors, mediators, degradation mechanisms and transformation products (TPs) of PhACs. In brief, higher hydrophobicity and having electron-donating groups, such as amine and hydroxyl in molecular structure leads to more effective degradation of PhACs by fungal cultures. For recalcitrant compounds, using redox mediators, such as syringaldehyde increases the degradation efficiency, however they may cause toxicity in the effluent and deactivate the enzyme. Immobilization of enzymes on supports can enhance the performance of enzyme in terms of reusability and stability. However, the immobilization strategy should be carefully selected to reduce the cost and enable regeneration. Still, further studies are needed to elucidate the mechanisms involved in enzymatic degradation and the toxicity levels of TPs and also to optimize the whole treatment strategy to have economical and technical competitiveness.

Biocatalytic treatment with oxidoreductase enzymes, especially laccases are an environmentally benign method for biodegradation of pharmaceutical compounds, such as carbamazepine to less harmful compounds. However, enzymes are required to be immobilized on supports to be reusable and maintain their activity. Functionalization of support prior to immobilization of enzyme is highly important because of biomolecule-support interface on enzyme activity and stability. In this work, the effect of oxidation of nanobiochar, a carbonaceous material produced by biomass pyrolysis, using HCl, HSO, HNO and their mixtures on immobilization of laccase has been studied. Scanning electron microscopy indicated that the structure of nanobiochars remained intact after oxidation and Fourier transform infrared spectroscopy confirmed the formation of carboxylic groups because of acid treatment. Titration measurements showed that the sample treated with HSO/HNO (50:50, v/v) had the highest number of carboxylic groups (4.7mmol/g) and consequently the highest efficiency for laccase immobilization. Additionally, it was observed that the storage, pH and thermal stability of immobilized laccase on functionalized nanobiochar was improved compared to free laccase showing its potential for continuous applications. The reusability tests towards oxidation of 2, 2'-azino-bis (3-ethylbenzothiazoline-6-sulphonic acid) (ABTS) showed that the immobilized laccase preserved 70% of the initial activity after 3cycles. Finally, using immobilized laccase for degradation of carbamazepine exhibited 83% and 86% removal in spiked water and secondary effluent, respectively.

Lipase is one of the most widely used enzymes and plays an important role in biotechnological and industrial processes including food, paper, and oleochemical industries, as well as in pharmaceutical applications. However, its aqueous solubility and instability make its application relatively difficult and expensive. The immobilization technique is often used to improve lipase performance, and the strategy has turned out to be a promising method. Immobilized lipase on nanomaterials (NMs) has shown superiority to the free lipase, such as improved thermal and pH stability, longer stable time, and the capacity of being reused. However, immobilization of lipase on NMs also sometimes causes activity loss and protein loading is relatively lowered under some conditions. The overall performance of immobilized lipase on NMs is influenced by mechanisms of immobilization, type of NMs being used, and physicochemical features of the used NMs (such as particle size, aggregation behavior, NM dimension, and type of coupling/modifying agents being used). Based on the specific features of lipase and NMs, this review discusses the recent developments, some mechanisms, and influence of NMs on lipase immobilization and their activity. Multiple application potential of the immobilized lipases has also been considered.

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