Biomolecule-engineered metal-organic frameworks (Bio-MOFs) are designed by incorporating biomolecules into or onto MOFs through covalent and non-covalent interactions. These composite frameworks exhibit unique catalytic and biological activities, making them highly suitable for various biocatalytic applications. In this review, we highlight recent advances in the material design, bioengineering methods, structural and functional regulation techniques, and biocatalytic applications of Bio-MOFs. From a materials perspective, we explore their unique structures and multifunctional properties, including high surface area, tunable pore sizes, and excellent biocompatibility. We also discuss various bioengineering techniques such as biomineralization and post-synthetic modification that are employed for their synthesis. Furthermore, we examine the structural and functional regulations of Bio-MOFs, which enhance catalytic activity and stability through interactions with enzymes, peptides, and other biomolecules. Finally, we analyze their applications in diverse biocatalytic reactions, including biosensors/sensors, drug delivery, catalytic therapy, organic wastewater purification, and emerging bio-energy science. This review underscores the pivotal role of biomolecules in enhancing the biocatalytic functions of MOFs and aims to inspire the design and synthesis of novel Bio-MOFs for future bio-related applications.
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http://dx.doi.org/10.1002/tcr.202500001 | DOI Listing |
Chem Rec
March 2025
College of Chemistry & Chemical Engineering, Qingdao University, Qingdao, 266071, China.
Biomolecule-engineered metal-organic frameworks (Bio-MOFs) are designed by incorporating biomolecules into or onto MOFs through covalent and non-covalent interactions. These composite frameworks exhibit unique catalytic and biological activities, making them highly suitable for various biocatalytic applications. In this review, we highlight recent advances in the material design, bioengineering methods, structural and functional regulation techniques, and biocatalytic applications of Bio-MOFs.
View Article and Find Full Text PDFAngew Chem Int Ed Engl
March 2025
University College Dublin, School of Chemistry, Belfield, 4, Dublin, IRELAND.
Biocatalysis is now a well-established branch of catalysis and the growing toolbox of natural, evolved and designer enzymes is enabling chemistry previously deemed inaccessible. However, most enzyme methodologies have been developed for functional group interconversions, such as the conversion of a ketone to an amine or alcohol, and do not result in the generation of significant 3D molecular complexity. The application of enzyme-triggered reaction cascade methodologies has the potential to transform simple substrates into complex sp3-rich molecules in one step.
View Article and Find Full Text PDFBiochim Biophys Acta Gen Subj
March 2025
Department of Applied Biological Chemistry, Graduate School of Agriculture, Osaka Metropolitan University, Sakai 599-8531, Japan. Electronic address:
Compartmentalization of multiple enzymes in cellulo and in vitro is a means of controlling the cascade reaction of metabolic enzymes. The compartmentation of enzymes through liquid-liquid phase separation may facilitate the reversible control of biocatalytic cascade reactions, thereby reducing the transcriptional and translational burden. This has attracted attention as a potential application in bioproduction.
View Article and Find Full Text PDFNat Chem
March 2025
School of Chemistry and Materials Science, Hangzhou Institute for Advanced Study, University of Chinese Academy of Sciences, Hangzhou, China.
Synthetic organic chemists continually draw inspiration from biocatalytic processes to innovate synthetic methodologies beyond existing catalytic platforms. Within this context, although 1,2-amino migration represents a viable biochemical process, it remains underutilized within the synthetic organic chemistry community. Here we present a biomimetic 1,2-amino migration accomplished through the synergistic combination of biocatalytic mechanism and photoredox catalysis.
View Article and Find Full Text PDFJ Nat Prod
March 2025
State Key Laboratory of Tropical Oceanography, Key Laboratory of Tropical Marine Bioresources and Ecology, Guangdong Key Laboratory of Marine Materia Medica, South China Sea Institute of Oceanology, Chinese Academy of Sciences, Guangzhou 510301, People's Republic of China.
-Methyltransferases involved in indole methylation have seldom been discovered in natural product biosynthesis. This study focuses on the enzyme CyaF, which catalyzes a critical -methylation step of indole in the β-carboline skeleton during cyanogramide biosynthesis. Seven β-carboline analogues (-) were isolated from the recombinant strain YF11/, including three new compounds (-).
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