Enzymatic biocatalysis is a sustainable technology. Enzymes are versatile and highly efficient biocatalysts, and have been widely employed due to their biodegradable nature. However, because the three-dimensional structure of these enzymes is predominantly maintained by weaker non-covalent interactions, external conditions, such as temperature and pH variations, as well as the presence of chemical compounds, can modify or even neutralize their biological activity. The enablement of this category of processes is the result of the several advances in the areas of molecular biology and biotechnology achieved over the past two decades. In this scenario, metal–organic frameworks (MOFs) are highlighted as efficient supports for enzyme immobilization. They can be used to ‘house’ a specific enzyme, providing it with protection from environmental influences. This review discusses MOFs as structures; emphasizes their synthesis strategies, properties, and applications; explores the existing methods of using immobilization processes of various enzymes; and lists their possible chemical modifications and combinations with other compounds to formulate the ideal supports for a given application.

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The Chemistry and Applications of Metal–Organic Frameworks (MOFs) as Industrial Enzyme Immobilization Systems

A stepwise docking and molecular dynamics approach for enzymatic biolubricant production using Lipase Eversa® Transform as a biocatalyst

Improvement of enzymatic activity and stability of lipase A from Candida antartica onto halloysite nanotubes with Taguchi method for optimized immobilization

In this study, a Taguchi experimental design was used for optimzing the immobilization of the lipase Eversa® Transform 2.0 (EVS) onto a hybrid support consisting of chitosan (CHI) and agarose (AGA), with glutaraldehyde (GLU) used as the support activator. The biocatalyst obtained was characterized by X-Ray Diffraction (XRD), Fourier Transform Infrared Spectroscopy (FTIR), Thermogravimetry (TGA), Energy Dispersive Spectroscopy (EDS), and Scanning Electron Microscopy (SEM). The optimized reaction conditions (60 min, 5 mM ionic strength, 1% GLU concentration, and 5 mg protein load per g of support) resulted in a highly active biocatalyst (74.39 ± 0.48 U/g) and delivered an immobilization yield of 74.20 ± 0.28%. The biocatalyst produced was observed to lose only 15.3% of its activity after 61 days of storage. The activity was also observed to increase by 96.70% ± 0.76, 27.34% ± 2.34, and 84.35% ± 1.68 in the presence of the organic solvents hexane, cyclohexane, and methanol, respectively. Additionally, the byocatalist showed more pronounced activity at temperatures above 50 °C and was still able to retain approximately 30% of it at 70 °C. These values were found to be higher at alkaline pHs, as the activity of Eversa® 2.0 Transform saw an increase of up to 140% at pH 9. The desorption tests performed did not reveal any enzymatic detachment from the support. The novel biocatalyst also showed promising ester-lubricating properties. Furthermore, the in silico study revealed a binding affinity of −5.1 kcal/mol between oleic acid and the enzyme, suggesting that the combination of the substrate and the lipase was more stable and therefore, suitable for esterification. 

A novel hybrid biocatalyst from immobilized Eversa® Transform 2.0 lipase and its application in biolubricant synthesis

This article conducted an advanced and comprehensive scientometric analysis of worldwide trends in decolorizing synthetic dyes by laccase. Articles were collected, analyzed, and classified according to the different substrates, enzymes, supports, immobilization procedures, and reactors involved. These studies were carried out in 200 institutions across 58 countries, with only 10 concentrating 88% of the total publications. China, India, and Turkey were identified as the main contributors to this research theme. Additionally, 26% of the institutions surveyed published only one article in the analyzed period. The results of the presented analysis encompassed data generated from 1999 to 2021, spanning more than two decades of specialized research. A ranking of article publications in scientific journals involving laccase, immobilization, enzymes, and dyes is listed. Also listed are the ranking of the 10 most prolific countries in the area of immobilized enzymes and the 10 most cited articles on the immobilization of enzymes with dyes. This analysis includes information related to the methods of support and costs of manufacture involving enzyme and immobilization routes. Finally, a discussion is presented exploring the fact that innovative technologies have been developed to render enzyme production more sustainable and economically viable. 

A scientometric analysis of research progress and trends in the design of laccase biocatalysts for the decolorization of synthetic dyes

Kaolin is a mineral composed of hydrated aluminum silicates, clayey and with high bioavailability. The choice of this mineral as immobilization matrix took into account these aspects mentioned above and its high surface area conducive to enzymatic immobilization, containing many OH- binding groups on its surface. Subsequently, the kaolin was functionalized with carboxymethylcellulose and polyethyleneimine (K-CMC-BPEI) and activated with Glutaraldehyde (K-CMC-BPEI-GLU) as a support to immobilize CAL-A. The [email protected] was characterized by X-Ray Diffraction (XRD), Fourier Transform Infrared Spectroscopy (FTIR), Thermogravimetry (TGA), and Scanning Electron Microscopy (SEM). [email protected], in the temperature range of 50–80 ºC, has a half-life 2–3 times longer than soluble CAL-A, that is, the immobilization process conferred greater stability thermal to the biocatalyst. Furthermore, docking studies showed that the immobilization of CAL-A on the support surface was favorable, since CAL-A has binding affinity to the protein-anchored ligand, estimated at −4.3 to −3.7 kcal/mol. Experiments were performed to verify the catalytic potential of [email protected] at a kinetic resolution of rac-1-(triisopropylsilyl) penta-1,4-diyn-3-ol (1) in an organic medium via an acylation reaction. All experiments yielded the product ((R)-1-Ac) with an excellent enantiomeric excess (ee >99%) and enantioselectivity (E > 200). 

Chemical modification of clay nanocomposites for the improvement of the catalytic properties of Lipase A from Candida antarctica

In recent years, the demand for sustainable energy resources has grown more and more, and with that, researchers around the world have been working to develop green technologies and products. Thus, biolubricants have emerged as a promising alternative to petroleum-derived lubricants, as they are characterized as fatty alcohol esters derived from vegetable oil. Therefore, they are biodegradable, non-toxic and guarantee easy disposal in the environment. Thus, some alternatives for its production have been studied. Among them, the use of enzymatic biocatalysts, mainly of the lipase class, offers an excellent alternative, as their reactions generally allow more significant energy efficiency and produce less waste than the conventional routes of chemical catalysts. Therefore, based on studies described in the literature, this article seeks to address the different aspects of the production of biolubricants catalyzed by lipases, highlighting the different reactions and sources of raw materials and presenting alternatives to improve these process protocols: enzymatic immobilization, alcohols and bioreactors. • The use of lipases in synthesizing biolubricant offers a cleaner alternative than chemical catalysts. • Enzymatic transesterification is an alternative technique for the production of high-performance biolubricants. • Biocatalysts produced without support have attracted attention to biolubricants synthesis. • The enzymatic synthesis of lubricant must continue to be carried out to balance production and expenditure. • The application of lipases produces cleaner biolubricants, reducing costs and making them more sustainable. 

Jeferson Yves Nunes Holanda Alexandre

Papers

A stepwise docking and molecular dynamics approach for enzymatic biolubricant production using Lipase Eversa® Transform as a biocatalyst

Chemical modification of clay nanocomposites for the improvement of the catalytic properties of Lipase A from Candida antarctica

Renewable processes of synthesis of biolubricants catalyzed by lipases