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Magnetic chitosan nanoparticles, synthesized by in situ precipitation, have been used as adsorbents to remove sulfamethoxazole (SMX), a sulfonamide antibiotic dangerous due to its capacity to enter ecosystems. The adsorption of SMX has been carried out in the presence of tertiary wastewaters from a depuration plant to obtain more realistic results. The effect of pH on the adsorption capacity significantly changed when carrying out the experiments in the presence of wastewater. This change has been explained while taking into account the charge properties of both the antibiotic and the magnetic chitosan. The composition of wastewaters has been characterized and discussed as regards its effect on the adsorption capacity of the magnetic chitosan. The models of Elovich and Freundlich have been selected to describe the adsorption kinetics and the adsorption isotherms, respectively. The analysis of these models has suggested that the adsorption mechanism is based on strong chemical interactions between the SMX and the magnetic chitosan, leading to the formation of an SMX multilayer.

A significant bottleneck for the industrial application of lipases stems from their poor stability in the presence of commercial triglycerides. This is mainly due to the inactivating effect of the products of triglyceride oxidation (PTO), which are usually produced when oils and fats, being imported from far countries, are stored for long periods. In this study, the immobilization of a lipase from Candida rugosa on chitosan hydrogels has been carried out following two alternative approaches based on the enzyme adsorption and entrapment to increase the lipase stability under the operating conditions that are typical of oleochemical transformations. The effect of model compounds representing different classes of PTO on a lipase has been studied to optimize the enzyme immobilization method. Particular attention has been devoted to the characterization of the inactivating effect of PTO in nonaqueous media, which are adopted for most industrial applications of lipases.

Dyes are considered as one the most important classes of contaminants that threaten the environment and human life. The synergy between the adsorption capacity of chitosan hydrogels and the catalytic properties of the enzyme laccase was exploited to improve the removal of contaminants from a liquid stream. The adsorption capacity of a chitosan hydrogel was tested on three different textile dyes. The effect of pH on the adsorption efficiency was dependent on the dye tested: the removal of methylene blue (MB), a cationic dye, was more effective at alkaline values of pH, whereas bromophenol blue (BPB) and Coomassie brilliant blue (BB), both anionic dyes, were more effectively removed under acid environments. The use of laccase immobilized onto chitosan has significantly improved the efficiency of dye removal, exploiting the synergy between the adsorption capacity of chitosan and the catalytic properties of the enzyme. The simultaneous processes of adsorption and enzymatic degradation improved the dye removal whatever the pH value adopted, making the removal efficiency less dependent from the pH changes. The chitosan used as a support for the immobilization of laccases showed good stability under repeated cycles, demonstrating the feasibility of the method developed for the application in wastewater remediation.

Three-dimensional chitosan-gallic acid complexes were proposed and prepared for the first time by a simple adsorption process of gallic acid (GA) on three-dimensional chitosan structures (3D chitosan). Highly porous 3D devices facilitate a high GA load, up to 2015 mmol/kg at pH 4.0. The preservation of the redox state of GA released from 3D chitosan was confirmed by spectroscopic analyses. The antioxidant activity of 3D chitosan-GA complexes was assessed using the DPPH radical scavenging assay and was found to be dramatically higher than that of free chitosan. The mechanical property of 3D chitosan-GA complexes was also evaluated using a compression test. Finally, 3D chitosan-GA complexes showed a significant antimicrobial capacity against E. coli and S. aureus , selected, respectively, as a model strain for Gram-negative and Gram-positive bacteria. Our study demonstrated a new, simple, and eco-friendly approach to prepare functional chitosan-based complexes for nutraceutical, cosmeceutical, and pharmaceutical applications.

Mesoporous silica materials offer a unique opportunity for enzyme immobilization thanks to their properties, such as tuneable pore size, large surface area and easy functionalization. However, a significant enhancement of cellulase enzyme activity entrapped inside the silica pores still represents a challenge. In this work, we immobilized cellulase by adsorption on wrinkled silica nanoparticles (WSNs), obtaining an active and stable biocatalyst. We used pentanol as co-solvent to synthesize WSNs with enhanced inter-wrinkle distance in order to improve cellulase hosting. The physical-chemical and morphological characterization of WSNs and cellulase/WSNs was performed by thermogravimetric (TG), Fourier transform infrared (FT-IR), and transmission electron microscopy (TEM) analyses. The obtained results showed that this matrix generates a favourable microenvironment for hosting cellulase. The results of the catalytic assays and operational stability confirmed the key role of size, morphology and distribution of the pores in the successful outcome of the cellulase immobilization process. The immobilization procedure used allowed preserving most of the secondary structure of the enzyme and, consequently, its catalytic activity. Moreover, the same value of glucose yield was observed for five consecutive runs, showing a high operational stability of the biocatalyst.

An immobilization protocol of a model enzyme into silica nanoparticles was applied. This protocol exploited the use of the bifunctional molecule triethoxysilylpropylisocyanate (TEPI) for covalent binding through a linker of suitable length. The enzyme β-glucosidase (BG) was anchored onto wrinkled silica nanoparticles (WSNs). BG represents a bottleneck in the conversion of lignocellulosic biomass into biofuels through cellulose hydrolysis and fermentation. The key aspect of the procedure was the use of an organic solvent (anhydrous acetone) in which the enzyme was not soluble. This aimed to restrict its conformational changes and thus preserve its native structure. This approach led to a biocatalyst with improved thermal stability, characterized by high immobilization efficiency and yield. It was found that the apparent K M value was about half of that of the free enzyme. The V max was about the same than that of the free enzyme. The biocatalyst showed a high operational stability, losing only 30% of its activity after seven reuses., Competing Interests: The authors declare no conflict of interest.