The enzymatic processes are increasingly highlights, especially in the synthesis of chemical products with high added value. The enzyme immobilization can improve industrial biocatalytic processes. The immobilization of enzymes provides the production of efficient, stable biocatalysts, possibility of reuse and easy purification of the products, when compared to the free enzymes. There is a growing research for more efficient methods of enzyme immobilization. In this context, the choice of support and immobilization strategy can significantly improve the final enzymatic properties. In this review paper, we aimed to discuss the versatility of biocatalysts immobilized enzymes design, focusing on the opportunities and disadvantages for each method presented. They discussed the recent development of enzyme immobilization methods and applications relating the final properties of the produced biocatalysts with the desired goals.

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In this study, biodiesel was produced through the enzymatic esterification of vegetable oils from two common Brazilian palm trees: babassu and tucuman. The oils were hydrolyzed by a chemical route and their free fatty acids esterified with ethanol and methanol using the lipase enzyme Eversa® Transform 2.0 in free forms and supported in iron magnetic nanoparticles (Fe3O4) (enzymatic load: 80 UpNPBg−1). These enzymatic reactions were performed at an oil–alcohol molar ratio of 1:1, reaction temperature of 37 °C, agitation at 150 rpm, and reaction times of 2, 4, 6 and 8 h for the reactions catalyzed by the soluble enzyme and 8 h for the reactions using the biocatalyst. The conversions of fatty acids in ethyl and methyl esters obtained were monitored by gas chromatography (CG). The results obtained from ester synthesis using enzyme catalysts in free form were better: babassu 52.6% (methanol) and 57.5% (ethanol), and for tucuman 96.7% (methanol) and 93.4% (ethanol). In the case of immobilized enzymes, the results obtained ranged from 68.7% to 82.2% for babassu and from 32.5% to 86.0% for tucuman, with three cycles of reuse and without significant catalyst loss. Molecular coupling studies revealed the structures of lipase and that linoleic acid bonded near the active site of the enzyme with the best free energy of −6.5 Kcal/mol.

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The unique properties of metal-organic frameworks (MOFs) such as their large surface area and high porosity have attracted considerable attention in recent decades. The MOFs are a promising class of materials for developing highly efficient biosensors due to these same properties. This bibliometric analysis focused on the use of MOFs as enzyme-coupled materials in biosensor construction and aimed to provide a comprehensive overview of the research field by analyzing a collected database. The analysis included identifying the countries that have published the most, the most prominent applications, and trends for future directions in the field. The study used three databases with different numbers of documents, differentiated by research areas, with refinements made to the search as needed. The results suggest that MOF-derived biosensors are a growing field, with the Republic of China emerging as a significant contributor to research in this area. The study also used computational processing of trend analysis and geocoding to reveal these findings.