ArticleACS ES&T water2024
Natural Silicates Encapsulated Enzymes as Green Biocatalysts for Degradation of Pharmaceuticals.
Article in ACS ES&T water, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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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, 7 citations in OpenAlex.
- Fly ash upcycling to functional silica nanomaterials: insights into synthetic strategies towards efficient adsorbents for water purification.RSC advances · 2025Article
- Hybrid Double Enzyme Biocatalyst for Effective Degradation of Organic Pollutants.ACS environmental Au · 2025Article
- Visualizing Catalytic Oxidation of Tryptophan by Nanoceria via an Oligonuclear Cerium Oxo-Complex Model.Inorganic chemistry · 2025Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Biocatalytic degradation with the use of enzymes has gained great attention in the past few years due to its advantages of high efficiency and environmental friendliness. Novel, cost-effective, and green nanoadsorbents were produced in this study, using natural silicates as an enzyme host matrix for core-shell immobilization technique. With the natural silicate as a core and silica layer as a shell, it was possible to encapsulate two different enzymes: horseradish peroxidase (HRP) and laccase, for removal and degradation of three pharmaceuticals: diclofenac (DFC), carbamazepine (CBZ), and paracetamol (PC). The biocatalysts demonstrated high oxidation rates for the selected pollutants. In particular HRP immobilized fly ash and perlite degraded DFC and PC completely during 3 days of interaction and also showed high degradation rates for CBZ. Immobilized laccase was successful in PC degradation, where up to 70-80% degradation of the compounds with aromatic rings was reported by NMR measurements for a high drug concentration of 10 μg/mL. The immobilization method played a significant role in this process by providing stability and protection for the enzymes over 3 weeks. Furthermore, the enzymes acted differently in the three chosen supports due to their complex chemical composition, which could have an effect on the overall enzyme activity.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.