This review comprehensively explores natural polymer-based materials, focusing on their characteristics, applications, and innovations across different sectors, including medicine, the environment, energy, textiles, and construction. With increasing concern about resource depletion and pollution, biomaterials offer a sustainable alternative to fossil-derived products. The review highlights polysaccharide-based and protein-based biomaterials, as well as others, such as polyisoprene, rosin, and hyaluronic acid. Emphasis is laid on their compositions and attractive characteristics, including biocompatibility, biodegradability, and functional versatility. Moreover, the review deeply discusses the ability of natural polymers to form hydrogels, aerogels, films, nanocomposites, etc., enhanced by additives for innovative applications. Future development trends of biomaterials in biomedicine, sustainable materials, environmental biotechnology, and advanced manufacturing are also explored. Their growing potential in these sectors is driven by research advances in emerging technologies such as 3D bioprinting, nanotechnology, and hybrid material innovation, which are proven to enhance the performance, functionality, and scalability of biopolymers. The review suggests several strategies, including improvement in processing techniques and material engineering to overcome limitations associated with biomaterials, thereby reinforcing their suitability and role in a circular and sustainable economy.

Currently, great attention is focused on conducting manufacture processes using clean and eco-friendly technologies. This research trend also relates to the production of immobilized biocatalysts of industrial importance using matrices and methods that fulfill specified operational and environmental requirements. For that reason, hydrogels of natural origin and the entrapment method become increasingly popular in terms of enzyme immobilization. The presented work is the comparative research on invertase immobilization using two natural hydrogel matrices—alginate and gelatin. During the study, we provided the molecular insight into the structural characteristics of both materials regarding their applicability as effective enzyme carriers. In order to confirm our predictions of using these hydrogels for invertase immobilization, we performed the typical experimental studies. In this case, the appropriate conditions of enzyme entrapment were selected for both types of carrier. Next, the characterization of received invertase preparations was made. As a final experimental result, the gelatin-based hydrogel was selected as an effective carrier for invertase immobilization. Hereby, using mild conditions and a pro-ecological, biodegradable matrix, it was possible to obtain very stable and reactive biocatalyst. The choice of gelatin-immobilized invertase preparation was compatible with our predictions based on the molecular models of hydrogel matrices and enzyme used.

This study presents a thorough overview of metal–organic frameworks’ (MOFs) utility as supports for enzyme immobilization. It details a bibliometric analysis of the field from 2014–2023, based on 911 Web of Science articles. Research outlines the functional properties of MOFs, the enzyme groups, and common immobilization techniques. It showcases diverse enzyme-MOF combinations for numerous applications, including industrial biocatalysis, medical diagnostics, drug development, biomass conversion, environmental protection, and biosensor creation. Current development trends and future directions are identified through literature analysis. Latent Dirichlet Allocation (LDA) modeling revealed key research themes over the years, highlighting shifts in focus towards advanced catalytic methods and adsorption techniques. Additionally, a word cloud generated for 2024 publications indicates an increasing emphasis on specialized applications involving ZIFs, nanoparticles, and magnetic structures. Key future perspectives include new MOF materials, such as biologically derived MOFs, core–shell magnetic hierarchical porous MOFs, nanoMOFs, and mesoporous MOFs. Novel materials inspired by MOF carriers, such as covalent organic frameworks (COFs) and metal–organic aerogels (MOAs), are also highlighted. Lastly, the study emphasizes the potential for multienzymatic systems and multifunctional MOF-enzyme composites, facilitating multiple functionalities within a single system.

Hydroxylation of L-tyrosine to 3,4-dihydroxyphenylalanine (L-DOPA) by immobilized tyrosinase in the presence of ascorbic acid (AH₂), which reduces DOPA-quinone to L-DOPA, is characterized by low reaction yields that are mainly caused by the suicide inactivation of tyrosinase by L-DOPA and AH₂. The main aim of this work was to compare processes with native and immobilized tyrosinase to identify the conditions that limit suicide inactivation and produce substrate conversions to L-DOPA of above 50% using HPLC analysis. It was shown that immobilized tyrosinase does not suffer from partitioning and diffusion effects, allowing a direct comparison of the reactions performed with both forms of the enzyme. In typical processes, additional aeration was applied and boron ions to produce the L-DOPA and AH₂ complex and hydroxylamine to close the cycle of enzyme active center transformations. It was shown that the commonly used pH 9 buffer increased enzyme stability, with concomitant reduced reactivity of 76%, and that under these conditions, the maximal substrate conversion was approximately 25 (native) to 30% (immobilized enzyme). To increase reaction yield, the pH of the reaction mixture was reduced to 8 and 7, producing L-DOPA yields of approximately 95% (native enzyme) and 70% (immobilized). A three-fold increase in the bound enzyme load achieved 95% conversion in two successive runs, but in the third one, tyrosinase lost its activity due to strong suicide inactivation caused by L-DOPA processing. In this case, the cost of the immobilized enzyme preparation is not overcome by its reuse over time, and native tyrosinase may be more economically feasible for a single use in L-DOPA production. The practical importance of the obtained results is that highly efficient hydroxylation of monophenols by tyrosinase can be obtained by selecting the proper reaction pH and is a compromise between complexation and enzyme reactivity.