Similar Publications

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 PDF

Hierarchical materials: An overview of synthesis methods and revolutionary impact on enzyme biocatalysis.

Colloids 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 PDF

Rieske Oxygenases: Powerful Models for Understanding Nature's Orchestration of Electron Transfer and Oxidative Chemistry.

Biochemistry

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 PDF

Illuminating the universe of enzyme catalysis in the era of artificial intelligence.

Cell 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 PDF

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.

View Article and Find Full Text PDF