This critical review focuses on the origins and preparation of bio-based surfactants, defined here as non-soap, amphiphilic molecules in which the carbon atoms are derived from annually renewable feedstocks. Environmental concerns and market pressures have led to greater relevance of these chemicals in commercial applications in recent years and extensive research has gone into exploring new classes of surfactants. Highlighted here are examples of bio-based surfactants that are produced on an industrial scale and/or are based on abundant starting materials. The trend of increasing use of renewable resources as starting materials for surfactants is introduced, followed by extensive discussion of the major classes of bio-derived hydrophobes and hydrophiles. Also discussed is the status of research and development with regard to biosynthetically produced surfactants. Finally, concluding remarks address the potential for new surfactant molecular structures as a result of ongoing development in the chemistry of biorefineries, i.e., that the transformation of lignocellulose into fuels is likely to support the manufacturing of new bio-based coproducts (238 references).
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.
Cyanotoxins removal are dependent on environmental parameters, mainly pH and Natural Organic Matters Chlorination and ozonation employed for cyanotoxin treatment may breach guideline values Membrane technology and photocatalysis operation involves high energy and maintenance Specific reaction pathway shifts oxidation process more towards sustainable approach
A B S T R A C TCarbamazepine (CBZ) is one of the most detected pharmaceutical compounds around the world, with adverse human and animal health impacts in wastewater effluents. Recently, biocatalytic degradation using ligninolytic enzymes such as laccase along with redox mediators provides a promising approach for their removal from water and wastewater. However, the effects of operational parameters on biotransformation need to be investigated in order to design a robust and efficient process. In this research, central composite design was performed and analyzed using response surface methodology to study the effects of temperature, pH, enzyme concentration and mediator concentration. The adequacy of the developed model was confirmed by the coefficient of multiple regression (R 2 = 75.97%) indicating a reasonable model for practical implementation. The results showed that performing the biotransformation at 35°C, pH 6, with 60 U/L of enzyme concentration and 18 μM of mediator concentration resulted in 95% removal of CBZ. 10,11-Dihydro-10,11-dihydroxy-CBZ and 10,11-dihydro-10,11epoxy-CBZ were identified as the major metabolites of CBZ oxidation by laccase. The estrogenicity tests indicated that the CBZ with an initial concentration of 4 μM and its biotransformation products had no estrogenic effect. The successful transformation of CBZ demonstrated the potential of the laccase-mediator system for the removal of recalcitrant micro-contaminants. (S.K. Brar).Process Biochemistry xxx (xxxx) xxx-xxx 1359-5113/
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