Biodiesel can be produced from vegetable oils, animal fats, frying oils, and from microorganism-synthesized oils. These sources render biodiesel an easily biodegradable fuel. The aim of this work was to perform an advanced bibliometric analysis of primary studies relating to biodiesel production worldwide by identifying the key countries and regions that have shown a strong engagement in this area, and by understanding the dynamics of their collaboration and research outputs. Additionally, an assessment of the main primary feedstocks employed in this research was carried out, along with an analysis of the current and future trends that are expected to define new paths and methodologies to be used in the manufacture of biodegradable and renewable fuels. A total of 4586 academic outputs were selected, including peer-reviewed research articles, conference papers, and literature reviews related to biodiesel production, in the time period spanning from 2010 to 2021. Articles that focused on feedstocks for the production of biodiesel were also included, with a search that returned 330 papers. Lastly, 60 articles relating to biodiesel production via sewage were specifically included to allow for an analysis of this source as a promising feedstock in the future of the biofuel market. Via the geocoding and the document analyses performed, we concluded that China, Malaysia, and India are the largest writers of articles in this area, revealing a great interest in biofuels in Asia. Additionally, it was noted that environmental concerns have caused authors to conduct research on feedstocks that can address the sustainability challenges in the production of biodiesel.

The synthesis of ethyl butyrate catalyzed by lipases A (CALA) or B (CALB) from Candida antarctica immobilized onto magnetic nanoparticles (MNP), CALA-MNP and CALB-MNP, respectively, is hereby reported. MNPs were prepared by co-precipitation, functionalized with 3-aminopropyltriethoxysilane, activated with glutaraldehyde, and then used as support to immobilize either CALA or CALB (immobilization yield: 100 ± 1.2% and 57.6 ± 3.8%; biocatalysts activities: 198.3 ± 2.7 U_p-NPB/g and 52.9 ± 1.7 U_p-NPB/g for CALA-MNP and CALB-MNP, respectively). X-ray diffraction and Raman spectroscopy analysis indicated the production of a magnetic nanomaterial with a diameter of 13.0 nm, whereas Fourier-transform infrared spectroscopy indicated functionalization, activation and enzyme immobilization. To determine the optimum conditions for the synthesis, a four-variable Central Composite Design (CCD) (biocatalyst content, molar ratio, temperature and time) was performed. Under optimized conditions (1:1, 45 °C and 6 h), it was possible to achieve 99.2 ± 0.3% of conversion for CALA-MNP (10 mg) and 97.5 ± 0.8% for CALB-MNP (12.5 mg), which retained approximately 80% of their activity after 10 consecutive cycles of esterification. Under ultrasonic irradiation, similar conversions were achieved but at 4 h of incubation, demonstrating the efficiency of ultrasound technology in the enzymatic synthesis of esters.

A theoretical and experimental study was carried out on the biocatalytic production of babassu biodiesel through enzymatic hydroesterification. The complete hydrolysis of babassu oil was carried out using a 1:1 mass solution at 40 °C for 4 h using 0.4% of lipase from Thermomyces lanuginosus (TLL). Then, with the use of Eversa^® Transform 2.0 lipase in the esterification step, a statistical design was used, varying the temperature (25–55 °C), the molar ratio between free fatty acids (FFAs) and methanol (1:1 to 1:9), the percentage of biocatalyst (0.1% to 0.9%), and the reaction time (1–5 h) using the Taguchi method. The ideal reaction levels obtained after the statistical treatment were 5 h of reaction at 40 °C at a molar ratio of 1:5 (FFAs/methanol) using 0.9% of the biocatalyst. These optimal conditions were validated by chromatographic analysis; following the EN 14103 standard, the sample showed an ester concentration of 95.76%. A theoretical study was carried out to evaluate the stability of Eversa with FFAs. It was observed in the molecular docking results that the ligands interacted directly with the catalytic site. Through molecular dynamics studies, it was verified that there were no significant conformational changes in the studied complexes. Theoretical and experimental results show the feasibility of this process.

Lignocellulosic biomasses are used in several applications, such as energy production, materials, and biofuels. These applications result in increased consumption and waste generation of these materials. However, alternative uses are being developed to solve the problem of waste generated in the industry. Thus, research is carried out to ensure the use of these biomasses as enzymatic support. These surveys can be accompanied using the advanced bibliometric analysis tool that can help determine the biomasses used and other perspectives on the subject. With this, the present work aims to carry out an advanced bibliometric analysis approaching the main studies related to the use of lignocellulosic biomass as an enzymatic support. This study will be carried out by highlighting the main countries/regions that carry out productions, research areas that involve the theme, and future trends in these areas. It was observed that there is a cooperation between China, USA, and India, where China holds 28.07% of publications in this area, being the country with the greatest impact in the area. Finally, it is possible to define that the use of these new supports is a trend in the field of biotechnology.

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.

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. GRAPHICAL ABSTRACT