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Rationally tailoring a controlled spatial organization of enzymes in a nanoarchitecture for multi-enzyme cascade reactions can enhance the catalytic efficiency via substrate channeling. However, attaining substrate channeling is a grand challenge, requiring sophisticated techniques. Herein, we report facile polymer-directed metal-organic framework (MOF)-based nanoarchitechtonics for realizing a desirable enzyme architecture with significantly enhanced substrate channeling. The new method involves the use of poly(acrylamide-co-diallyldimethylammonium chloride) (PADD) as a modulator in a one-step process for simultaneous MOF synthesis and co-immobilization of enzymes (GOx and HRP). The resultant enzymes-PADD@MOFs constructs showed a closely packed nanoarchitecture with enhanced substrate channeling. A transient time close to 0 s was observed, owing to a short diffusion path for substrates in a 2D spindle-shaped structure and their direct transfer from one enzyme to another. This enzyme cascade reaction system showed a 3.5-fold increase in catalytic activity in comparison to free enzymes. The findings provide a new insight into using polymer-directed MOF-based enzyme nanoarchitectures to improve catalytic efficiency and selectivity.
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http://dx.doi.org/10.1021/acs.langmuir.3c00879 | DOI Listing |
Micron
September 2025
IMEC, Kapeldreef 75, Leuven 3001, Belgium.
The epitaxial growth of semiconductor multilayers often starts from monocrystalline wafers that have an offcut angle. This offcut angle is critical for tailoring the properties of epitaxial materials, making its precise control essential. This study demonstrates a novel approach to determine the wafer offcut angle based on electron channeling patterns (ECP) obtained by scanning electron microscopy.
View Article and Find Full Text PDFPlant Physiol Biochem
September 2025
Department of Agricultural, Food and Nutritional Science, University of Alberta, Edmonton, Alberta, T6G 2P5, Canada. Electronic address:
Many plant-derived unusual fatty acids (UFAs) possess valuable chemical properties and have potential applications in the food, feed, and oleochemical industries. Despite significant interest, the mechanisms by which plants synthesize and accumulate these structurally distinct fatty acids remain only partially understood. While enzyme substrate specificities involved in UFA-containing storage lipid assembly have been well characterized in many prior studies, the biochemical roles of protein-protein interactions (PPIs) in coordinating UFA biosynthesis have received less attention.
View Article and Find Full Text PDFbioRxiv
August 2025
Roy and Diana Vagelos Laboratories, Department of Chemistry, University of Pennsylvania, Philadelphia, Pennsylvania, 19104-6323, USA.
Copalyl diphosphate synthase from (PvCPS) is a bifunctional class II terpene synthase containing a prenyltransferase that produces geranylgeranyl diphosphate (GGPP) and a class II cyclase that utilizes GGPP as a substrate to generate the bicyclic diterpene copalyl diphosphate. The various stereoisomers of copalyl diphosphate establish the greater family of labdane natural products, many of which have environmental and medicinal impact. Understanding structure-function relationships in class II diterpene synthases is crucial for guiding protein engineering campaigns aimed at the generation of diverse bicyclic diterpene scaffolds.
View Article and Find Full Text PDFChem Sci
August 2025
Natural Product Biosynthesis Research Unit, RIKEN Center for Sustainable Resource Science Wako Saitama 351-0198 Japan
Terpene cyclases (TCs), consisting of various combinations of α, β, and γ domains, have been extensively studied. Recently, non-canonical enzymes comprising a TCβ domain and a haloacid dehalogenase (HAD)-like domain (referred to as HAD-TCβ) have been discovered. However, their overall structure remains unclear.
View Article and Find Full Text PDFJ Environ Manage
August 2025
University Bremen, Bibliothekstraße 1, Bremen, 28359, Germany.
In response to climate change, the expansion of renewable energies leads to an increasing number of offshore wind farms in the North Sea. This comes along with an increase in (artificial) hard substrates in a mainly soft-bottom dominated marine area with so far largely unknown consequences for the underlying ecosystem functioning. We used a large combined dataset (both hard- and soft-substrate data) to model the secondary production of fouling communities on turbine foundations and of soft-bottom fauna inside and outside offshore wind farms (OWF) in the southern North Sea (Belgium, the Netherlands, Germany).
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