Naturally occurring substances or polymeric biomolecules synthesized by living organisms during their entire life cycle are commonly defined as biopolymers. Different classifications of biopolymers have been proposed, focusing on their monomeric units, thus allowing them to be distinguished into three different classes with a huge diversity of secondary structures. Due to their ability to be easily manipulated and modified, their versatility, and their sustainability, biopolymers have been proposed in different fields of interest, starting from food, pharmaceutical, and biomedical industries, (i.e., as excipients, gelling agents, stabilizers, or thickeners). Furthermore, due to their sustainable and renewable features, their biodegradability, and their non-toxicity, biopolymers have also been proposed in wastewater treatment, in combination with different reinforcing materials (natural fibers, inorganic micro- or nano-sized fillers, antioxidants, and pigments) toward the development of novel composites with improved properties. On the other hand, the improper or illegal emission of untreated industrial, agricultural, and household wastewater containing a variety of organic and inorganic pollutants represents a great risk to aquatic systems, with a negative impact due to their high toxicity. Among the remediation techniques, adsorption is widely used and documented for its efficiency, intrinsic simplicity, and low cost. Biopolymers represent promising and challenging adsorbents for aquatic environments’ decontamination from organic and inorganic pollutants, allowing for protection of the environment and living organisms. This review summarizes the results obtained in recent years from the sustainable removal of contaminants by biopolymers, trying to identify open questions and future perspectives to overcome the present gaps and limitations.

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.

˙O₂⁻superoxide radicals are firmly adsorbed on the surface of the hybrid material giving oxidative degradation without any light irradiation.

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.