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• Sonochemistry was employed to synthesize cysteine-coated magnetite, enabling versatile enzyme immobilization. • Fe 3 O 4 @LC-CALA nanoparticles have an approximate size of 11.1±2.4 nm. • The biocatalyst system exhibited superior thermal stability and pH tolerance compared to free CALA. This study presents the synthesis of magnetite nanoparticles coated with L-cysteine (Fe 3 O 4 @LC) and their subsequent utilization as a support matrix for the immobilization of Candida antarctica Lipase A (CALA). The immobilization process involved physical interactions and covalent bonding mediated by glutaraldehyde. Comprehensive characterization was conducted using techniques including X-ray diffraction (XRD), transmission electron microscopy (TEM), scanning electron microscopy (SEM), Fourier-transform infrared spectroscopy (FTIR), X-ray photoelectron spectroscopy (XPS), and vibrating sample magnetometry (VSM), providing compelling evidence of a successful synthesis. Under optimized conditions, employing 1 mg of protein per gram of support, pH 7 in a 25 mM phosphate buffer, and a 5 h reaction at 25 °C, immobilization on glutaraldehyde-activated support achieved an impressive yield of 85.0 % ± 2.6, accompanied by a specific activity of 212.5 ± 1.3 U/g, outperforming the physical adsorption approach. Remarkably, the immobilized enzyme exhibited higher activity than the free enzyme at alkaline and acidic pH levels. Furthermore, thermal and pH inactivation studies revealed that the biocatalyst's half-life exceeded that of free CALA by more than 8 times at pH 10. These results underscore the potential of the Fe 3 O 4 @LC-GLU-CALA system as a robust biocatalytic matrix with promising applications in biodiesel production, ester synthesis, and pharmaceutical manufacturing. [Display omitted] [ABSTRACT FROM AUTHOR]

Magnetic biocatalysts combine magnetic properties with the catalytic activity of enzymes, achieving easy recovery and reuse in biotechnological processes. Lipases immobilized by magnetic nanoparticles dominate. This review covers an advanced bibliometric analysis and an overview of the area, elucidating research advances. Using WoS, 34,949 publications were analyzed and refined to 450. The prominent journals, countries, institutions, and authors that published the most were identified. The most cited articles showed research hotspots. The analysis of the themes and keywords identified five clusters and showed that the main field of research is associated with obtaining biofuels derived from different types of sustainable vegetable oils. The overview of magnetic biocatalysts showed that these materials are also employed in biosensors, photothermal therapy, environmental remediation, and medical applications. The industry shows a significant interest, with the number of patents increasing. Future studies should focus on immobilizing new lipases in unique materials with magnetic profiles, aiming to improve the efficiency for various biotechnological applications. [Display omitted] • Research progress, trends, and updates on magnetic biocatalysts were investigated. • The growing interest in research into magnetic biocatalysts is described. • The application of magnetic biocatalysts over the last 12 years was studied. • Comprehensive guidelines are given for magnetic biocatalyst research. • The most and least used raw materials for producing magnetic biocatalysts were investigated. [ABSTRACT FROM AUTHOR]

Highlights • The review deals with the current state the of art of lipases from Pseudomonas. • The production and properties of lipases from Pseudomonas are discussed. • Many strategies of immobilization of lipases from Pseudomonas are presented. • Lipases from Pseudomonas potential in biotechnological applications is outlined. Abstract Lipases from Pseudomonas are extracellular enzymes that play an important role in biotechnological and industrial processes, due to their application in biofuels, food and pharmaceutical industries. Therefore, this paper provides an overview about the main aspects of the lipases from Pseudomonas, regarding their catalytic characterization, production, immobilization and application in many reactions of high industrial interest. The catalytic characterization and production of the lipase will be discussed, including the main lipase properties available in the literature and the influence of media composion, making possible the optimization of lipase production. Based on the main features of the lipases from Pseudomonas , this review also explores the recent developments on strategies of immobilization in order to enable recovery operations of the biocatalyst. The application of lipases to production of many high added-value products through esterifications, hydrolysis reactions and resolution of racemic compounds was also explored. The high yield and enantioselectivity of their reactions, regarding the resolution of racemic mixtures, shows that the lipases from Pseudomonas are efficient biocatalysts for biotechnological processes. [ABSTRACT FROM AUTHOR]