ArticleMaterials (Basel, Switzerland)2020
Direct Exposure of Dry Enzymes to Atmospheric Pressure Non-Equilibrium Plasmas: The Case of Tyrosinase.
Article in Materials (Basel, Switzerland), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 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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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
2 citing papers in PubMed, 8 citations in OpenAlex.
- Dielectric Barrier Plasma Discharge Exsolution of Nanoparticles at Room Temperature and Atmospheric Pressure.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- Atmospheric Pressure Plasmas in Material Science.Materials (Basel, Switzerland) · 2021Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
Abstract
The direct interaction of atmospheric pressure non-equilibrium plasmas with tyrosinase (Tyr) was investigated under typical conditions used in surface processing. Specifically, Tyr dry deposits were exposed to dielectric barrier discharges (DBDs) fed with helium, helium/oxygen, and helium/ethylene mixtures, and effects on enzyme functionality were evaluated. First of all, results show that DBDs have a measurable impact on Tyr only when experiments were carried out using very low enzyme amounts. An appreciable decrease in Tyr activity was observed upon exposure to oxygen-containing DBD. Nevertheless, the combined use of X-ray photoelectron spectroscopy and white-light vertical scanning interferometry revealed that, in this reactive environment, Tyr deposits displayed remarkable etching resistance, reasonably conferred by plasma-induced changes in their surface chemical composition as well as by their coffee-ring structure. Ethylene-containing DBDs were used to coat tyrosinase with a hydrocarbon polymer film, in order to obtain its immobilization. In particular, it was found that Tyr activity can be fully retained by properly adjusting thin film deposition conditions. All these findings enlighten a high stability of dry enzymes in various plasma environments and open new opportunities for the use of atmospheric pressure non-equilibrium plasmas in enzyme immobilization strategies.
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Registered trials
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