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https://olympias.lib.uoi.gr/jspui/handle/123456789/39805Full metadata record
| DC Field | Value | Language |
|---|---|---|
| dc.contributor.author | Zampara, Stefania | en |
| dc.contributor.author | Ζαμπάρα, Στεφανία | el |
| dc.date.accessioned | 2026-02-27T11:39:16Z | - |
| dc.date.available | 2026-02-27T11:39:16Z | - |
| dc.identifier.uri | https://olympias.lib.uoi.gr/jspui/handle/123456789/39805 | - |
| dc.rights | Attribution-NonCommercial-NoDerivs 3.0 United States | * |
| dc.rights.uri | http://creativecommons.org/licenses/by-nc-nd/3.0/us/ | * |
| dc.subject | Enzymes | en |
| dc.subject | Nanobiotechnology | en |
| dc.subject | Carbon-based nanomaterials | en |
| dc.subject | Green synthetic methods | en |
| dc.subject | Bio-graphene structural studies | en |
| dc.subject | Ένζυμα | el |
| dc.subject | Νανοβιοτεχνολογία | el |
| dc.subject | Νανοϋλικά άνθρακα | el |
| dc.subject | Πράσινη συνθετική πορεία | el |
| dc.subject | Βιογραφένιο | el |
| dc.subject | Δομικές μελέτες | el |
| dc.title | Study of the structure and function of enzymes in carbon nanomaterials | en |
| dc.title | Μελέτη της σχέσης δομής και λειτουργίας ενζύμων σε νανοϋλικά άνθρακα | el |
| dc.type | masterThesis | en |
| heal.type | masterThesis | el |
| heal.type.en | Master thesis | en |
| heal.type.el | Μεταπτυχιακή εργασία | el |
| heal.classification | Biotechnology | en |
| heal.classification | Βιοτεχνολογία | el |
| heal.dateAvailable | 2026-02-27T11:40:18Z | - |
| heal.language | en | el |
| heal.access | free | el |
| heal.recordProvider | Πανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών | el |
| heal.publicationDate | 2026-02-26 | - |
| heal.abstract | Enzymes are essential biological macromolecules whose activity and stability are strongly influenced by their structural integrity and their interaction with the surrounding environments. In recent years, carbon-based nanomaterials have attracted significant attention as promising platforms for enzyme immobilization due to their unique physicochemical properties, high surface area, and potential to enhance enzyme performance. The present study focuses on the investigation of the structure and function of two important enzymes, lysozyme and α-amylase, following their immobilization on graphene oxide and two environmentally friendly nanomaterials, bio-graphene and magnetic bio-graphene. The primary objective of this work was to examine how the interaction between these enzymes and carbon nanomaterials affects their functional characteristics. Enzyme immobilization on nanomaterial surfaces can influence protein folding, stability, and activity through physicochemical interactions such as electrostatic forces, hydrogen bonding, and surface adsorption. Understanding these interactions is essential for the development of advanced nanobiotechnological applications, including biosensors, biocatalytic systems, and biomedical devices. To further investigate these effects, spectroscopic techniques were employed to monitor potential structural and conformational changes in the enzymes’ molecules. Ultraviolet–visible (UV–Vis) absorption spectroscopy was used to evaluate changes in the electronic environment of the enzymes and to confirm their interaction with the nanomaterials. Fluorescence spectroscopy provided valuable information regarding alterations in the tertiary structure and the microenvironment of aromatic amino acid residues, allowing the detection of conformational modifications. Additionally, Circular Dichroism (CD) spectroscopy was utilized to analyze changes in the secondary structure of the enzymes, offering insight into variations in α-helix and β-sheet content induced by their interaction with graphene oxide, bio-graphene, and magnetic bio-graphene. The use of green nanomaterials such as bio-graphene and magnetic bio-graphene represents an important step toward more sustainable and biocompatible nanobiotechnological systems. These materials provide potential advantages, including enzyme stabilization, reusability, and environmentally friendly synthesis routes. The results of this study contribute to a better understanding of enzyme–nanomaterial interactions at the molecular level and highlight the potential of carbon-based nanomaterials as effective platforms for enzyme immobilization. Overall, this work provides valuable insight into the structural behavior of lysozyme and α-amylase in the presence of graphene-based nanomaterials, contributing to the broader field of nanobiotechnology and supporting the development of advanced functional nanomaterial–enzyme systems for future applications. | en |
| heal.advisorName | Σταμάτης, Χαράλαμπος | el |
| heal.committeeMemberName | Σταμάτης, Χαράλαμπος | el |
| heal.committeeMemberName | Καταπόδης, Πέτρος | el |
| heal.committeeMemberName | Πολύδερα, Αγγελική | |
| heal.academicPublisher | Πανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείας | el |
| heal.academicPublisherID | uoi | el |
| heal.numberOfPages | 101 | el |
| heal.fullTextAvailability | true | - |
| Appears in Collections: | Διατριβές Μεταπτυχιακής Έρευνας (Masters) - ΧΗΜ | |
Files in This Item:
| File | Description | Size | Format | |
|---|---|---|---|---|
| Μ.Ε. Ζαμπάρα Στεφανία (2026).pdf | 2.45 MB | Adobe PDF | View/Open |
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