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Biocatalysis offers a sustainable approach to drug synthesis, leveraging the high selectivity and efficiency of enzymes. This review explores the application of biocatalysis in the early-stage synthesis of antimicrobial compounds, emphasizing its advantages over traditional chemical methods. We discuss various biocatalysts, including enzymes and whole-cell systems, and their role in the selective functionalization and preparation of antimicrobials and antibacterial building blocks. The review underscores the potential of biocatalysis to advance the development of new antibiotics and suggests directions and potential applications of enzymes in drug development.
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http://dx.doi.org/10.1039/d4ra04824e | DOI Listing |
Microb Cell Fact
August 2025
Molecular Plant Biology Unit, Department of Life Technologies, University of Turku, Turku, Finland.
Cyanobacteria are emerging as a promising platform for whole-cell biotransformation, harnessing solar energy to drive biocatalytic reactions through recombinant enzymes. However, optimisation remains challenging due to the complexity of the cyanobacterial metabolism and the regulatory framework in which heterologous enzymes operate. While many enzymes have been deployed for light-driven whole-cell biotransformations, the different experimental conditions used between studies make direct comparison and systematic improvement difficult.
View Article and Find Full Text PDFColloids Surf B Biointerfaces
August 2025
Department of Food Science, Cornell University, Ithaca, NY 14853, USA. Electronic address:
Enzymes are exceptional biological catalysts given their high substrate specificity and ability to accelerate chemical reactions under mild conditions. To harness the potential of enzymes outside their native environments, immobilization technologies continue to emerge enhancing enzyme stability and handling. Insoluble materials have been widely used as enzyme supports, and their composition and structure usually determine the performance of the resulting biocatalysts.
View Article and Find Full Text PDFBiochemistry
August 2025
Department of Chemical and Pharmaceutical Biology, Groningen Research Institute of Pharmacy, University of Groningen, Antonius Deusinglaan 1, Groningen 9713AV, Netherlands.
Rieske oxygenases (ROs) are a diverse family of nonheme iron enzymes that catalyze a wide array of oxidative transformations in both catabolic and biosynthetic pathways. Their catalytic repertoire spans dioxygenation, monooxygenation, oxidative - and -dealkylation, desaturation, sulfoxidation, C-C bond formation, -oxygenation, and C-N bond cleavage─reactions that are often challenging to achieve selectively through synthetic methods. These diverse functions highlight the increasing importance of ROs in natural product biosynthesis and establish them as promising candidates for biocatalytic applications.
View Article and Find Full Text PDFCell Syst
August 2025
Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, CA 91125, USA; Division of Biology and Biological Engineering, California Institute of Technology, Pasadena, CA 91125, USA. Electronic address:
Scientific research has revealed only a minuscule fraction of the enzymes that evolution has generated to power life's essential chemical reactions-and an even tinier fraction of the vast universe of possible enzymes. Beyond the enzymes already annotated lie an astronomical number of biocatalysts that could enable sustainable chemical production, degrade toxic pollutants, and advance disease diagnosis and treatment. For the past few decades, directed evolution has been a powerful strategy for reshaping enzymes to access new chemical transformations: by harnessing nature's existing diversity as a starting point and taking inspiration from nature's most powerful design process, evolution, to modify enzymes incrementally.
View Article and Find Full Text PDFSmall
August 2025
Department of Chemistry, The University of Texas at Austin, 105 E 24th St., Austin, TX, 78712, USA.
Nanoparticles (NPs) are known to enhance the activity of enzymes, but such findings remain largely empirical, lacking predictive design principles. Here, the first high-throughput platform for the discovery of surface-engineered nanoparticles (SENs) that modulate enzyme function is introduced. Guided by the hypothesis that surface ligands are primary drivers of activity enhancement, a library of 194 gold- and palladium-based SENs functionalized with diverse peptide ligands is synthesized.
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