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1. DNA-enzyme nanostructures enhance enzyme stability and functionality

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   Lee, Seungheon; Samanta, Devleena (February 2025, Chem)
2. Single enzyme electroanalysis

   https://doi.org/10.1039/D1AN00230A  

   Vannoy, Kathryn J.; Ryabykh, Andrey; Chapoval, Andrei I.; Dick, Jeffrey E. (June 2021, The Analyst)

   Traditional studies of enzymatic activity rely on the combined kinetics of millions of enzyme molecules to produce a product, an experimental approach that may wash out heterogeneities that exist between individual enzymes. Evaluating these properties on an enzyme-by-enzyme basis represents an unambiguous means of elucidating heterogeneities; however, the quantification of enzymatic activity at the single-enzyme level is fundamentally limited by the maximum catalytic rate, k cat , inherent to a given enzyme. For electrochemical methods measuring current, single enzymes must turn over greater than 10 7 molecules per second to produce a measurable signal on the order of 10 −12 A. Enzymes with this capability are extremely rare in nature, with typical k cat values for biologically relevant enzymes falling between 1 and 10 000 s −1 . Thus, clever amplification strategies are necessary to electrochemically detect the vast majority of enzymes. This review details the progress toward the electroanalytical detection and evaluation of single enzyme kinetics largely focused on the nanoimpact method, a chronoamperometric detection strategy that monitors the change in the current-time profile associated with stochastic collisions of freely diffusing entities ( e.g. , enzymes) onto a microelectrode or nanoelectrode surface. We discuss the experimental setups and methods developed in the last decade toward the quantification of single molecule enzymatic rates. Special emphasis is given to the limitations of measurement science in the observation of single enzyme activity and feasible methods of signal amplification with reasonable bandwidth. 

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3. Parallels between enzyme catalysis, electrocatalysis, and photoelectrosynthesis

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   Nishiori, Daiki; Wadsworth, Brian L.; Moore, Gary F. (October 2021, Chem Catalysis)
4. Thioesterase enzyme families: Functions, structures, and mechanisms

   https://doi.org/10.1002/pro.4263  

   Caswell, Benjamin T.; Carvalho, Caio C.; Nguyen, Hung; Roy, Monikrishna; Nguyen, Tin; Cantu, David C. (March 2022, Protein Science)
5. One-pot synthesis of enzyme@metal–organic material (MOM) biocomposites for enzyme biocatalysis

   https://doi.org/DOI https://doi.org/10.1039/D1GC00775K  

   Pan, Y.; Li, H.; Lenertz, M.; Han, Y.; Ugrinov, A.; Kilin, D.; Chen, B.; Yang, Z. (March 2021, Green chemistry)

   null (Ed.)

   Metal–organic frameworks/materials (MOFs/MOMs) are advanced enzyme immobilization platforms that improve biocatalysis, materials science, and protein biophysics. A unique way to immobilize enzymes is co-crystallization/co-precipitation, which removes the limitation on enzyme/substrate size. Thus far, most enzyme@MOF composites rely on the use of non-sustainable chemicals and, in certain cases, heavy metals, which not only creates concerns regarding environmental conservation but also limits their applications in nutrition and biomedicine. Here, we show that a dimeric compound derived from lignin, 5,5′-dehydrodivanillate (DDVA), co-precipitates with enzymes and low-toxicity metals, Ca2+ and Zn2+, and forms stable enzyme@Ca/Zn–MOM composites. We demonstrated this strategy on four enzymes with different isoelectric points (IEPs), molecular weights, and substrate sizes. Furthermore, we found that all enzymes displayed slightly different but reasonable catalytic efficiencies upon immobilization in the Ca–DDVA and Zn–DDVA MOMs, as well as reasonable reusability in both composites. We then probed the structural basis of such differences using a representative enzyme and found enhanced restriction of enzymes in Zn–DDVA than in Ca–DDVA, which might have caused the activity difference. To the best of our knowledge, this is the first aqueous-phase, one-pot synthesis of a lignin-derived “green” enzyme@MOF/MOM platform that can host enzymes without any limitations on enzyme IEP, molecular weight, and substrate size. The different morphologies and crystallinities of the composites formed by Ca–DDVA and Zn–DDVA MOMs broaden their applications depending on the problem of interest. Our approach of enzyme immobilization not only improves the sustainability/reusability of almost all enzymes but also reduces/eliminates the use of non-sustainable resources. This synthesis method has a negligible environmental impact while the products are non-toxic to living things and the environment. The biocompatibility also makes it possible to carry out enzyme delivery/release for nutritional or biomedical applications via our “green” biocomposites. 

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