Chitosan, a copolymer of glucosamine and N-acetyl glucosamine, is derived from chitin. Chitin is found in cell walls of crustaceans, fungi, insects and in some algae, microorganisms, and some invertebrate animals. Chitosan is emerging as a very important raw material for the synthesis of a wide range of products used for food, medical, pharmaceutical, health care, agriculture, industry, and environmental pollution protection. This review, in line with the focus of this special issue, provides the reader with (1) an overview on different sources of chitin, (2) advances in techniques used to extract chitin and converting it into chitosan, (3) the importance of the inherent characteristics of the chitosan from different sources that makes them suitable for specific applications and, finally, (4) briefly summarizes ways of tailoring chitosan for specific applications. The review also presents the influence of the degree of acetylation (DA) and degree of deacetylation (DDA), molecular weight (M_w) on the physicochemical and biological properties of chitosan, acid-base behavior, biodegradability, solubility, reactivity, among many other properties that determine processability and suitability for specific applications. This is intended to help guide researchers select the right chitosan raw material for their specific applications.

Poly(ethylene 2,5-furanoate) (PEF) is arousing great interest as a biobased alternative to plastics like poly(ethylene terephthalate) (PET) due to its wide range of potential applications, such as food and beverage packaging, clothing, and in the car industry. In the present study, the hydrolysis of PEF powders of different molecular masses (M_n = 55, M_w = 104 kg/mol and M_n = 18, M_w = 29 kg/mol) and various particle sizes (180 < d and 180 < d < 425 µm) using cutinase 1 from Thermobifida cellulosilytica (Thc_cut1) was studied. Thereby, the effects of molecular mass, particle size and crystallinity on enzymatic hydrolysis were investigated. The results show that particles with lower molecular mass are hydrolyzed faster than those with higher masses, and that the higher the molecular mass, the lower the influence of the particle size on the hydrolysis. Furthermore, cutinases from Humicola insolens (HiC) and Thc_cut1 were compared with regard to their hydrolytic activity on amorphous PEF films (measured as release of 2,5-furandicarboxylic acid (FDCA) and weight loss) in different reaction media (1 M KPO pH 8, 0.1 M Tris-HCl pH 7) and at different temperatures (50 °C and 65 °C). A 100% hydrolysis of the PEF films was achieved after only 72 h of incubation with a HiC in 1 M KPO pH 8 at 65 °C. Moreover, the hydrolysis reaction was monitored by LC/TOF-MS analysis of the released reaction products and by Scanning Electron Microscopy (SEM) examination of the polymer surfaces. Enzymatic hydrolysis of PEF with Thc_cut1 and HiC has potential for use in surface functionalization and recycling purposes.

Polyurethanes (PU) are one of the most-used classes of synthetic polymers in Europe, having a considerable impact on the plastic waste management in the European Union. Therefore, they represent a major challenge for the recycling industry, which requires environmentally friendly strategies to be able to re-utilize their monomers without applying hazardous and polluting substances in the process. In this work, enzymatic hydrolysis of a polyurethane-polyester (PU-PE) copolymer using Humicola insolens cutinase (HiC) has been investigated in order to achieve decomposition at milder conditions and avoiding harsh chemicals. PU-PE films have been incubated with the enzyme at 50 °C for 168 h, and hydrolysis has been followed throughout the incubation. HiC effectively hydrolysed the polymer, reducing the number average molecular weight (M_n) and the weight average molecular weight (M_w) by 84% and 42%, respectively, as shown by gel permeation chromatography (GPC), while scanning electron microscopy showed cracks at the surface of the PU-PE films as a result of enzymatic surface erosion. Furthermore, Fourier Transform Infrared (FTIR) analysis showed a reduction in the peaks at 1725 cm⁻¹, 1164 cm⁻¹ and 1139 cm⁻¹, indicating that the enzyme preferentially hydrolysed ester bonds, as also supported by the nuclear magnetic resonance spectroscopy (NMR) results. Liquid chromatography time-of-flight/mass spectrometry (LC-MS-Tof) analysis revealed the presence in the incubation supernatant of all of the monomeric constituents of the polymer, thus suggesting that the enzyme was able to hydrolyse both the ester and the urethane bonds of the polymer.

In Europe, most of the discarded and un-wearable textiles are incinerated or landfilled. In this study, we present an enzyme-based strategy for the recovery of valuable building blocks from mixed textile waste and blends as a circular economy concept. Therefore, model and real textile waste were sequentially incubated with (1) protease for the extraction of amino acids from wool components (95% efficiency) and (2) cellulases for the recovery of glucose from cotton and rayon constituents (85% efficiency). The purity of the remaining poly(ethylene terephthalate) (PET) unaltered by the enzymatic treatments was assessed via Fourier-transformed infrared spectroscopy. Amino acids recovered from wool were characterized via elementary and molecular size analysis, while the glucose resulting from the cotton hydrolysis was successfully converted into ethanol by fermentation with Saccharomyces cerevisiae. This work demonstrated that the step-wise application of enzymes can be used for the recovery of pure building blocks (glucose) and their further reuse in fermentative processes.

A reliance on fossil fuel has led to the increased emission of greenhouse gases (GHGs). The excessive consumption of raw materials today makes the search for sustainable resources more pressing than ever. Technical lignins are mainly used in low-value applications such as heat and electricity generation. Green enzyme-based modifications of technical lignin have generated a number of functional lignin-based polymers, fillers, coatings, and many other applications and materials. These bio-modified technical lignins often display similar properties in terms of their durability and elasticity as fossil-based materials while also being biodegradable. Therefore, it is possible to replace a wide range of environmentally damaging materials with lignin-based ones. By researching publications from the last 20 years focusing on the latest findings utilizing databases, a comprehensive collection on this topic was crafted. This review summarizes the recent progress made in enzymatically modifying technical lignins utilizing laccases, peroxidases, and lipases. The underlying enzymatic reaction mechanisms and processes are being elucidated and the application possibilities discussed. In addition, the environmental assessment of novel technical lignin-based products as well as the developments, opportunities, and challenges are highlighted.

Cellulose acetate (CA)-based materials, like cigarette filters, contribute to landscape pollution challenging municipal authorities and manufacturers. This study investigates the potential of enzymes to degrade CA and to be potentially incorporated into the respective materials, enhancing biodegradation. Deacetylation studies based on Liquid Chromatography-Mass Spectrometry-Time of Flight (LC-MS-TOF), High Performance Liquid Chromatography (HPLC), and spectrophotometric analysis showed that the tested esterases were able to deacetylate the plasticizer triacetin (glycerol triacetate) and glucose pentaacetate (cellulose acetate model compound). The most effective esterases for deacetylation belong to the enzyme family 2 (AXE55, AXE 53, GAE), they deacetylated CA with a degree of acetylation of up to 1.8. A combination of esterases and cellulases showed synergistic effects, the absolute glucose recovery for CA 1.8 was increased from 15% to 28% when an enzymatic deacetylation was performed. Lytic polysaccharide monooxygenase (LPMO), and cellobiohydrolase were able to cleave cellulose acetates with a degree of acetylation of up to 1.4, whereas chitinase showed no activity. In general, the degree of substitution, chain length, and acetyl group distribution were found to affect CA degradation. This study shows that, for a successful enzyme-based deacetylation system, a cocktail of enzymes, which will randomly cleave and generate shorter CA fragments, is the most suitable.