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A wide array of organic compounds have been recognized as pollutants of high concern due to their controlled or uncontrolled presence in environmental matrices. The persistent prevalence of diverse organic pollutants, including pharmaceutical compounds, phenolic compounds, synthetic dyes, and other hazardous substances, necessitates robust measures for their practical and sustainable removal from water bodies. Several bioremediation and biodegradation methods have been invented and deployed, with a wide range of materials well-suited for diverse environments. Enzyme-linked carbon-based materials have been considered efficient biocatalytic platforms for the remediation of complex organic pollutants, mostly showing over 80% removal efficiency of micropollutants. The advantages of enzyme-linked carbon nanotubes (CNTs) in enzyme immobilization and improved catalytic potential may thus be advantageous for environmental research considering the current need for pollutant removal. This review outlines the perspective of current remediation approaches and highlights the advantageous features of enzyme-linked CNTs in the removal of pollutants, emphasizing their reusability and stability aspects. Furthermore, different applications of enzyme-linked CNTs in environmental research with concluding remarks and future outlooks have been highlighted. Enzyme-linked CNTs serve as a robust biocatalytic platform for the sustainability agenda with the aim of keeping the environment clean and safe from a variety of organic pollutants., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2023 Elsevier Inc. All rights reserved.)

Nanobiocatalysts, in which enzyme molecules are integrated into/onto multifunctional materials, such as metal-organic frameworks (MOFs), have been fascinating and appeared as a new interface of nanobiocatalysis with multi-oriented applications. Among various nano-support matrices, functionalized MOFs with magnetic attributes have gained supreme interest as versatile nano-biocatalytic systems for organic bio-transformations. From the design (fabrication) to deployment (application), magnetic MOFs have manifested notable efficacy in manipulating the enzyme microenvironment for robust biocatalysis and thus assure requisite applications in several areas of enzyme engineering at large and nano-biocatalytic transformations, in particular. Magnetic MOFs-linked enzyme-based nano-biocatalytic systems offer chemo-regio- and stereo-selectivities, specificities, and resistivities under fine-tuned enzyme microenvironments. Considering the current sustainable bioprocesses demands and green chemistry needs, we reviewed synthesis chemistry and application prospects of magnetic MOFs-immobilized enzyme-based nano-biocatalytic systems for exploitability in different industrial and biotechnological sectors. More specifically, following a thorough introductory background, the first half of the review discusses various approaches to effectively developed magnetic MOFs. The second half mainly focuses on MOFs-assisted biocatalytic transformation applications, including biodegradation of phenolic compounds, removal of endocrine disrupting compounds, dye decolorization, green biosynthesis of sweeteners, biodiesel production, detection of herbicides and screening of ligands and inhibitors., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2023 Elsevier B.V. All rights reserved.)

The synergistic combination of current biotechnological and nanotechnological research has turned to multienzyme co-immobilization as a promising concept to design biocatalysis engineering. It has also intensified the development and deployment of multipurpose biocatalysts, for instance, multienzyme co-immobilized constructs, via biocatalysis/protein engineering to scale-up and fulfil the ever-increasing industrial demands. Considering the characteristic features of both the loaded multienzymes and nanostructure carriers, i.e., selectivity, specificity, stability, resistivity, induce activity, reaction efficacy, multi-usability, high catalytic turnover, optimal yield, ease in recovery, and cost-effectiveness, multienzyme-based green biocatalysts have become a powerful norm in biocatalysis/protein engineering sectors. In this context, the current state-of-the-art in enzyme engineering with a synergistic combination of nanotechnology, at large, and nanomaterials, in particular, are significantly contributing and providing robust tools to engineer and/or tailor enzymes to fulfil the growing catalytic and contemporary industrial needs. Considering the above critics and unique structural, physicochemical, and functional attributes, herein, we spotlight important aspects spanning across prospective nano-carriers for multienzyme co-immobilization. Further, this work comprehensively discuss the current advances in deploying multienzyme-based cascade reactions in numerous sectors, including environmental remediation and protection, drug delivery systems (DDS), biofuel cells development and energy production, bio-electroanalytical devices (biosensors), therapeutical, nutraceutical, cosmeceutical, and pharmaceutical oriented applications. In conclusion, the continuous developments in nano-assembling the multienzyme loaded co-immobilized nanostructure carriers would be a unique way that could act as a core of modern biotechnological research., Competing Interests: Declaration of Competing Interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2023 Elsevier B.V. All rights reserved.)

With robust catalytic features, manganese peroxidases (MnPs) from various sources, including fungi and bacteria, have gained much consideration in many biotechnological applications with particular emphasis on environmental remediation. MnP is a heme-containing enzyme that belongs to the oxidoreductases that can catalyze the degradation of various organic pollutants, such as chlorophenols, nitroaromatic compounds, industrial dyes, and polycyclic aromatic hydrocarbons. To spotlight the MnP as biocatalytic tool, an effort has been put forward to cover the four major compartments. For instance, following a brief introduction, first, various microbial sources of MnP are discussed with examples. Second, structural attributes and biocatalytic features of MnP are given with examples. Third, different MnP immobilization strategies, including adsorption, covalent linking, entrapment, and cross-linking, are discussed with a significant motive to strengthen the enzyme's stability against diverse deactivation agents by restricting the conformational mobility of molecules. Compared to free counterparts, immobilized MnP fractions perform well in hostile environments. Finally, various biotechnological applications, such as fuel ethanol production, de-lignification, textile industry, pulp and paper industry, degradation of phenolic and non-phenolic compounds, and pharmaceutical and pesticide degradation, are briefly discussed., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2023 Elsevier B.V. All rights reserved.)

Nowadays, the specificity of enzymatic processes makes them more and more important every year, and their usage on an industrial scale seems to be necessary. Enzymatic cofactors, however, play a crucial part in the prospective applications of enzymes, because they are indispensable for conducting highly effective biocatalytic activities. Due to the relatively high cost of these compounds and their consumption during the processes carried out, it has become crucial to develop systems for cofactor regeneration. Therefore, in this review, an attempt was made to summarize current knowledge on enzymatic regeneration methods, which are characterized by high specificity, non-toxicity and reported to be highly efficient. The regeneration of cofactors, such as nicotinamide dinucleotides, coenzyme A, adenosine 5'-triphosphate and flavin nucleotides, which are necessary for the proper functioning of a large number of enzymes, is discussed, as well as potential directions for further development of these systems are highlighted. This review discusses a range of highly effective cofactor regeneration systems along with the productive synthesis of many useful chemicals, including the simultaneous renewal of several cofactors at the same time. Additionally, the impact of the enzyme immobilization process on improving the stability and the potential for multiple uses of the developed cofactor regeneration systems was also presented. Moreover, an attempt was made to emphasize the importance of the presented research, as well as the identification of research gaps, which mainly result from the lack of available literature on this topic., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2023 Elsevier B.V. All rights reserved.)

In recent decades, enzyme-based biocatalytic systems have garnered increasing interest in industrial and applied research for catalysis and organic chemistry. Many enzymatic reactions have been applied to sustainable and environmentally friendly production processes, particularly in the pharmaceutical, fine chemicals, and flavor/fragrance industries. However, only a fraction of the enzymes available has been stepped up towards industrial-scale manufacturing due to low enzyme stability and challenging separation, recovery, and reusability. In this context, immobilization and co-immobilization in robust support materials have emerged as valuable strategies to overcome these inadequacies by facilitating repeated or continuous batch operations and downstream processes. To further reduce separations, it can be advantageous to use multiple enzymes at once in one pot. Enzyme co-immobilization enables biocatalytic synergism and reusability, boosting process efficiency and cost-effectiveness. Several studies on multi-enzyme immobilization and co-localization propose kinetic advantages of the enhanced turnover number for multiple enzymes. This review spotlights recent progress in developing versatile biocatalytic cascade systems by multi-enzyme co-immobilization on environmentally friendly biopolymers and nanostructured materials and their application scope in the chemical and biotechnological industries. After a succinct overview of carrier-based and carrier-free immobilization/co-immobilizations, co-immobilization of enzymes on a range of biopolymer and nanomaterials-based supports is thoroughly compiled with contemporary and state-of-the-art examples. This study provides a new horizon in developing effective and innovative multi-enzymatic systems with new possibilities to fully harness the adventure of biocatalytic systems., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2022 Elsevier B.V. All rights reserved.)

Nanozymes are super-efficient nanomaterials with enzyme-like characteristics, as the name suggests. In the last decade, efforts have been made to develop "artificial enzymes," which are alternatives to natural enzymes. As nanoscience and nanotechnology advance, nanozymes, which are catalytic nanomaterials having enzyme-like properties, have fascinated researchers' attention. Nanozymes with unique physicochemical properties and nanomaterials that mimic catalytic activity have gained a special interest in the industrial sectors. However, several constraints have hampered their effective deployment in industrial processes, including denaturation, time-consuming manufacturing, overall high cost-ratio, and reutilization challenges. After a brief overview of nanozyme research, an analysis of the similarities and differences between nanozymes and natural and synthetic enzymes is presented. Because of their distinct properties, nanozymes stand out in this comparison. Nanozymes have exhibited a variety of applications leveraging the physiochemical properties of nanomaterials, ranging from in vitro detection to enzyme substitution in biological systems. In addition, nanozymes have introduced a new field called nanozymology, which blends nanotechnology with enzymology., Competing Interests: Declaration of Competing Interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2022 The Authors. Published by Elsevier B.V. All rights reserved.)

Nowadays, the increasing amounts of dyes present in wastewaters and even water bodies is an emerging global problem. In this work we decided to fabricate new biosystems made of nanofiltration or ultrafiltration membranes combined with laccase entrapped between polystyrene electrospun fibers and apply them for decolorization of aqueous solutions of three azo dyes, C.I. Acid Yellow 23 (AY23), C.I. Direct Blue 71 (DB71) and C.I. Reactive Black 5 (RB5). Besides effective decolorization of the permeate stream, the biosystems also allowed removal of dyes from the retentate stream as a result of enzymatic action. The effect of pH and applied pressure on decolorization efficiencies was investigated, and pH 5 and pressure of 2 bar gave the highest removal efficiencies of 97% for AY23 and 100% for both DB71 and RB5 from permeate solutions while decolorization of retentate for RB5 reached 65% under these conditions. Almost 100% decolorization of all dyes was achieved after three consecutive enzyme membrane cycles. Decolorization was shown to be due to the synergistic action of membrane separation and bioconversion. The biocatalytic action also enabled significant reduction of permeate and retentate toxicity, which is one of the biggest environmental health issues for these types of streams., (Copyright © 2022 Elsevier B.V. All rights reserved.)

The presence of micropollutants in water, wastewater and soil are a global problem due to their persistent effect on ecosystems and human health. Although there are many methods of removal of environmental pollutants, they are often ineffective for degradation of pharmaceuticals, including estrogens. In presented work we proposed fabrication of electrospun material from polyacrylonitrile/polyethersulfone (PAN/PES) as a support for laccase immobilization by covalent binding. Oxidoreductase was attached to the electrospun fibers using polydopamine as a linker and produced system was used for degradation of two estrogens: 17β-estradiol (E2) and 17α-ethynylestradiol (EE2). It was shown that 92% of E2 and 100% of EE2 were degraded after 24 h of the process. Moreover, the effect of surfactants, metal ions and mediators on conversion efficiencies of estrogens was investigated and it was confirmed that immobilized enzyme possessed higher resistance to inhibitory agents as well as thermal and storage stability, compared to its native form. Finally, estrogenic activities of E2 and EE2 solutions decreased around 99% and 87%, respectively, after enzymatic conversion, that corresponds to significant reduction of the total organic carbon and formation of low-toxic final products of estrogens degradation., (Copyright © 2022 Elsevier B.V. All rights reserved.)

In this study, we present the concept of co-immobilization of xylose dehydrogenase and alcohol dehydrogenase from Saccharomyces cerevisiae on an XN45 nanofiltration membrane for application in the process of xylose bioconversion to xylonic acid with simultaneous cofactor regeneration and membrane separation of reaction products. During the research, the effectiveness of the co-immobilization of enzymes was confirmed, and changes in the properties of the membrane after the processes were determined. Using the obtained biocatalytic system it was possible to obtain 99% xylonic acid production efficiency under optimal conditions, which were 5 mM xylose, 5 mM formaldehyde, ratio of NAD+:NADH 1:1, and 60 min of reaction. Additionally, the co-immobilization of enzymes made it possible to improve stability of the co-immobilized enzymes and to carry out xylose conversion in six consecutive cycles and after 7 days of storage at 4 °C with over 90% efficiency. The presented data confirm the effectiveness of the co-immobilization, improvement of the stability and reusability of the biocatalysts, and show that the obtained enzymatic system is promising for use in xylose bioconversion and simultaneous regeneration of nicotinamide cofactor., (Copyright © 2022 The Author(s). Published by Elsevier Inc. All rights reserved.)

Immobilized enzymes find applications in many areas such as pharmacy, medicine, food production and environmental protection. However, protecting these biocatalysts against harsh reaction conditions and retaining their enzymatic activity even after several biocatalytic cycles are major challenges. Properly selected supports and type of surface modifier therefore seem to be crucial for achieving high retention of catalytic activity of immobilized biomolecules. Here we propose production of novel composite electrospun fibers from polystyrene/poly(d,l-lactide-co-glycolide) (PS/PDLG) and its application as a support for immobilization of oxidoreductases such as alcohol dehydrogenase (ADH) and laccase (LAC). Two strategies of covalent binding, (i) (3-aminopropyl)triethoxysilane (APTES) with glutaraldehyde (GA) and (ii) polydopamine (PDA), were applied to attach oxidoreductases to PS/PDLG. The average fiber diameter was shown to increase from 1.252 µm to even 3.367 µm after enzyme immobilization. Effective production of PS/PDLG fibers and biomolecule attachment were confirmed by Fourier transform infrared spectroscopy analysis. The highest substrate conversion efficiency was observed at pH 6.5 and 5 for ADH and LAC, respectively, and at 25 °C for enzymes attached using the APTES + GA approach. Improvement of enzyme stabilization at high temperatures was confirmed in that relative activities of enzymes immobilized onto PS/PDLG fibers were over 20% higher than those of the free biomolecules, and enzyme leaching from the support using acetate and MES buffers was below 10 mg/g., (Copyright © 2021 The Author(s). Published by Elsevier Inc. All rights reserved.)

Anaerobic co-digestion (AcoD) can utilise spare digestion capacity at existing wastewater treatment plants (WWTP) to generate surplus biogas beyond the plant's internal energy requirement. Data from industry reports and the peer-reviewed literature show that through AcoD, numerous examples of WWTPs have become net energy producers, necessitating other high-value applications for surplus biogas. A globally emerging trend is to upgrade biogas to biomethane, which can then be used as town gas or transport fuel. Water, organic solvent and chemical scrubbing, pressure swing adsorption, membrane separation, and cryogenic technology are commercially available CO 2 removal technologies for biogas upgrade. Although water scrubbing is currently the most widely applied technology due to low capital and operation cost, significant market growth in membrane separation has been seen over the 2015-2019 period. Further progress in materials engineering and sciences is expected and will further enhance the membrane separation competitiveness for biogas upgrading. Several emerging biotechnologies to i) improve biogas quality from AcoD; ii) accelerate the absorption rate, and iii) captures CO 2 in microalgal culture have also been examined and discussed in this review. Through a combination of AcoD and biogas upgrade, more WWTPs are expected to become net energy producers., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2020 Elsevier B.V. All rights reserved.)

Composite polycaprolactone-chitosan material was produced by an electrospinning method and used as a support for immobilization of tyrosinase by mixed ionic interactions and hydrogen bonds formation. The morphology of the fibers and enzyme deposition were confirmed by SEM images. Further, multivariate polynomial regression was used to model the experimental data and to determine optimal conditions for immobilization process, which were found to be pH 7, temperature 25 °C and 16 h process duration. Under these conditions, novel type of biocatalytic system was produced with immobilization yield of 93% and expressed activity of 95%. Furthermore, as prepared system was applied in batch experiments related to biodegradation of bisphenol A under various remediation conditions. It was found that over 80% of the pollutant was removed after 120 min of the process, in the temperature range 15-45 °C and pH 6-9, using solutions at concentration up to 3 mg/L. Experimental data collected proved that the stability and reusability of the tyrosinase were significantly improved upon immobilization: the immobilized biomolecule retained around 90% of its initial activity after 30 days of storage, and was still capable to remove over 80% of bisphenol A even after 10 repeated uses. By contrast, free enzyme was able to remove over 80% of bisphenol A at pH 7-8 and temperature range 15-35 °C, and retained less than 60% of its initial activity after 30 days of storage., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2020 Elsevier B.V. All rights reserved.)

Novel electrospun poly(methyl methacrylate)/polyaniline electrospun fibres were produced, characterised, modified, and used as a support for laccase immobilisation by two methods: adsorption and covalent binding. Effective deposition of laccase by both methods was confirmed by FTIR and CLSM results. Nevertheless, the main objective of the study was to select the most favourable immobilisation conditions and prepare heterogeneous biocatalysts with the best possible catalytic properties. The highest relative activity of enzymes immobilised by adsorption and covalent binding were obtained after 1 h of immobilisation using laccase solution at a concentration of 1 mg/mL, at pH 5 and 25 °C. It was found that the immobilised enzymes, which were present in amounts of 110 mg/g and 185 mg/g for systems with adsorbed and covalently bonded laccase respectively, exhibited slightly lower substrate affinity, and in consequence also a lower maximum reaction rate, than the free enzyme. The stability of laccase improved significantly upon immobilisation: both heterogeneous biocatalysts retained over 80% relative activity even after 10 repeated catalytic cycles and 30 days of storage. The obtained systems were used for decolourisation of Remazol Brilliant Blue R dye from a model aqueous solution, resulting in removal efficiencies of 87% and 58% using adsorbed and covalently bonded laccase, respectively. The described approach to the removal of textile dye from model solution is significant for the sustainable and environmentally friendly decolourisation of various compounds from wastewater., Competing Interests: Declaration of competing interests The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2020 The Authors. Published by Elsevier Inc. All rights reserved.)

Enzymatic cofactor-dependent conversion of monosaccharides can be used in the bioproduction of value-added compounds. In this study, we demonstrate co-immobilization of xylose dehydrogenase (XDH, EC 1.1.1.175) and alcohol dehydrogenase (ADH, EC 1.1.1.1) using magnetite-silica core-shell particles for simultaneous conversion of xylose into xylonic acid (XA) and in situ cofactor regeneration. The reaction conditions were optimized by factorial design, and were found to be: XDH:ADH ratio 2:1, temperature 25 °C, pH 7, and process duration 60 min. Under these conditions enzymatic production of xylonic acid exceeded 4.1 mM and was more than 25% higher than in the case of a free enzymes system. Moreover, the pH and temperature tolerance as well as the thermo- and storage stability of the co-immobilized enzymes were significantly enhanced. Co-immobilized XDH and ADH make it possible to obtain higher xylonic acid concentration over broad ranges of pH (6-8) and temperature (15-35 °C) as compared to free enzymes, and retained over 60% of their initial activity after 20 days of storage. In addition, the half-life of the co-immobilized system was 4.5 times longer, and the inactivation constant (k D  = 0.0141 1/min) four times smaller, than those of the free biocatalysts (k D  = 0.0046 1/min). Furthermore, after five reaction cycles, immobilized XDH and ADH retained over 65% of their initial properties, with a final biocatalytic productivity of 1.65 mM of xylonic acid per 1 U of co-immobilized XDH. The results demonstrate the advantages of the use of co-immobilized enzymes over a free enzyme system in terms of enhanced activity and stability., (Copyright © 2019 Elsevier Inc. All rights reserved.)

Enzymatic biodegradation of pharmaceuticals, using enzymes such as laccase, is a green solution for the removal of toxic pollutants that has attracted growing interest over recent years. Moreover, the application of immobilized biocatalysts is relevant for industrial applications, due to the improved stability and reusability of the immobilized enzymes. Thus, in the present study, laccase was immobilized by adsorption and encapsulation using poly(l-lactic acid)-co-poly(ε-caprolactone) (PLCL) electrospun nanofibers as a tailor-made support. The produced biocatalytic systems were applied in the biodegradation of two commonly used anti-inflammatories, naproxen and diclofenac, which are present in wastewaters at environmentally relevant concentrations. The results showed that under optimal process conditions (temperature 25 °C, pH 5 and 3 for naproxen and diclofenac respectively), even from a solution at a concentration of 1 mg L -1 , over 90% of both pharmaceuticals was removed by encapsulated laccase in batch mode. Both immobilized enzymes also exhibited high reusability: after five reaction cycles approximately 60% and 40% of naproxen and diclofenac were removed by encapsulated and adsorbed laccase respectively. In addition, a thorough analysis was made of the products of biodegradation of the two studied pollutants. Furthermore, toxicity study of the mixture after biodegradation of the pharmaceuticals showed that the solutions obtained after the process were approximately 65% less toxic than the initial naproxen and diclofenac solutions., (Copyright © 2019 Elsevier B.V. All rights reserved.)

In the presented study synthesized magnetic nanoparticles were used as an inorganic precursor for the preparation of novel magnetite-lignin and magnetite-chitin hybrid supports for enzyme immobilization. Effective synthesis of the hybrids was confirmed by Fourier transform infrared spectroscopy and powder X-ray diffraction analysis. The materials exhibited good thermal stability and surface areas of 4.3 and 5.6 m 2 /g respectively. The magnetite-lignin + trypsin and magnetite-chitin + trypsin systems were found to have good storage stability and reusability. After 20 days they retained over 75% and 90% respectively of their initial activity, and after 10 consecutive biocatalytic cycles retained over 60% and 80% respectively of their initial activity. The kinetic parameters of the free and immobilized enzyme were also comprehensively examined and compared. The results of peptide digestion tests confirmed the high proteolytic activity of the produced trypsin-based magnetic biocatalytic systems., (Copyright © 2018 Elsevier B.V. All rights reserved.)

Bioremediation, a biologically mediated transformation or degradation of persistent chemicals into nonhazardous or less-hazardous substances, has been recognized as a key strategy to control levels of pollutants in water and soils. The use of enzymes, notably oxidoreductases such as laccases, tyrosinases, various oxygenases, aromatic dioxygenases, and different peroxidases (all of EC class 1) is receiving significant research attention in this regard. It should be stated that immobilization is emphasized as a powerful tool for enhancement of enzyme activity and stability as well as for protection of the enzyme proteins against negative effects of harsh reaction conditions. As proper selection of support materials for immobilization and their performance is overlooked when it comes to comparing performance of immobilized enzyme in academic studies, this review summarizes the current state of knowledge regarding the materials used for enzyme immobilization of these oxidoreductase enzymes for environmental applications. In the presented study, thorough physicochemical characteristics of the support materials was presented. Moreover, various types of reactions and notably operational modes of enzymatic processes for biodegradation of harmful pollutants are summarized, and future trends in use of immobilized oxidoreductases for environmental applications are discussed. Our goal is to provide an improved foundation on which new technological advancements can be made to achieve efficient enzyme-assisted bioremediation., (Copyright © 2018 Elsevier B.V. All rights reserved.)

Due to the rapid growth in quantities of phenolic compounds in wastewater, the development of efficient and environmentally friendly methods for their removal becomes a necessity. Thus, in a presented work, for the first time, a novel material, Hippospongia communis spongin-based scaffold, was used as a biopolymeric support for the immobilization of laccase from Trametes versicolor. The resulting biocatalytic systems were used for the biodegradation of three bisphenols: bisphenol A (BPA), bisphenol F (BPF) and bioremoval-resistant bisphenol S (BPS). Optimization of the immobilization and biodegradation methodologies was performed to increase bisphenols removal. The effect of temperature, pH and initial pollutant concentration was evaluated. It was shown that under optimal conditions, almost 100% of BPA (pH5, 30°C) and BPF (pH5, 40°C), and over 40% of BPS (pH4, 30°C) was removed from the solution at a concentration of 2mg/mL. Furthermore, the immobilized laccase exhibited good reusability and storage stability, retaining over 80% of its initial activity after 50days of storage. In addition, the main biodegradation products of BPA and BPF were identified. It was shown that mainly dimers and trimers were formed following the oxidation of bisphenols by the immobilized laccase., (Copyright © 2017 Elsevier B.V. All rights reserved.)

α-Amylase from Aspergillus oryzae was immobilized via covalent bonds and by physical interactions on a synthesized titania/lignin novel hybrid support. A temperature of 5°C, a pH of 7.0, an initial enzyme solution concentration of 3.0mg/mL and a 3h process duration were found to be optimal for the highest activity of the immobilized enzyme. Moreover, the effect of temperature, pH, storage time and repeated catalytic cycles on the activity of free and immobilized enzyme was examined. Bound α-amylase showed enhanced thermal and chemical stability, and its reusability was also improved. Immobilized α-amylase retained over 80% of its initial activity when stored for 30days at 4°C. Kinetic parameters of the free and immobilized biocatalyst were calculated and compared. The maximum reaction rate (V max ) and turnover number (k cat ) were slightly lower for the immobilized enzyme than for the free enzyme. It should be clearly stated that this work presents a useful protocol to produce stable and active immobilized α-amylase onto titania/lignin hybrid which may also be applied to immobilization of other enzymes., (Copyright © 2017 Elsevier B.V. All rights reserved.)

Advanced functional silica/lignin hybrid materials, modified with nanosilver, were obtained. The commercial silica Syloid 244 was used, modified with N-(2-aminoethyl)-3-aminopropyltrimethoxysilane to increase its chemical affinity to lignin. Similarly, kraft lignin was oxidized using a solution of sodium periodate to activate appropriate functional groups on its surface. Silver nanoparticles were grafted onto the resulting silica/lignin hybrids. The systems obtained were comprehensively tested using available techniques and methods, including transmission electron microscopy, Fourier transform infrared spectroscopy, energy-dispersive X-ray spectroscopy, elemental analysis and atomic absorption spectroscopy. An evaluation was also made of the electrokinetic stability of the systems with and without silver nanoparticles. Conclusions were drawn concerning the chemical nature of the bonds between the precursors and the effectiveness of the method of binding nanosilver to the hybrid materials. The antimicrobial activity of the studied materials was tested against five species of Gram-positive and Gram-negative bacteria. The addition of silver nanoparticles to the silica/lignin hybrids led to inhibition of the growth of the analyzed bacteria. The best results were obtained against Pseudomonas aeruginosa, a dangerous human pathogen., (Copyright © 2015 Elsevier B.V. All rights reserved.)