ArticleNanoscale research letters2011
Effect of substrate (ZnO) morphology on enzyme immobilization and its catalytic activity.
Article in Nanoscale research letters, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
3 citing papers in PubMed, 52 citations in OpenAlex.
- Green nanobiocatalysts: enhancing enzyme immobilization for industrial and biomedical applications.PeerJ · 2024Review
- Impacts of horseradish peroxidase immobilization onto functionalized superparamagnetic iron oxide nanoparticles as a biocatalyst for dye degradation.Environmental science and pollution research international · 2022Article
- Electrochemical route to the synthesis of ZnO microstructures: its nestlike structure and holding of Ag particles.Nanoscale research letters · 2013Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In this study, zinc oxide (ZnO) nanocrystals with different morphologies were synthesized and used as substrates for enzyme immobilization. The effects of morphology of ZnO nanocrystals on enzyme immobilization and their catalytic activities were investigated. The ZnO nanocrystals were prepared through a hydrothermal procedure using tetramethylammonium hydroxide as a mineralizing agent. The control on the morphology of ZnO nanocrystals was achieved by varying the ratio of CH3OH to H2O, which were used as solvents in the hydrothermal reaction system. The surface of as-prepared ZnO nanoparticles was functionalized with amino groups using 3-aminopropyltriethoxysilane and tetraethyl orthosilicate, and the amino groups on the surface were identified and calculated by FT-IR and the Kaiser assay. Horseradish peroxidase was immobilized on as-modified ZnO nanostructures with glutaraldehyde as a crosslinker. The results showed that three-dimensional nanomultipod is more appropriate for the immobilization of enzyme used further in catalytic reaction.
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Registered trials
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