| | SLO | ENG | Cookies and privacy

Bigger font | Smaller font

Show document Help

Title:Imobilizacija l-asparaginaze na magnetne nanodelce : magistrsko delo
Authors:ID Verdev, Maja (Author)
ID Leitgeb, Maja (Mentor) More about this mentor... New window
ID Primožič, Mateja (Comentor)
ID Vasić, Katja (Comentor)
Files:.pdf MAG_Verdev_Maja_2024.pdf (2,82 MB)
MD5: 3855B1E9A914CCF09F1F7DE09DECF1E7
 
Language:Slovenian
Work type:Master's thesis/paper
Typology:2.09 - Master's Thesis
Organization:FKKT - Faculty of Chemistry and Chemical Engineering
Abstract:V okviru zaključnega dela smo izvedli optimizacijo imobilizacije l-asparaginaze (l-ASNaze) na aminoksilanske magnetne nanodelce (AMN-MNPs). Postopek imobilizacije sestoji iz dveh korakov, funkcionalizacije AMN-MNPs in imobilizacije encima. V prvem koraku smo funkcionalizirali AMN-MNPs, v drugem koraku smo nanje imobilizirali l-ASNazo. Najprej smo v teoretičnem delu opisali lastnosti l-ASNaze, prikazali njeno strukturo, mehanizem delovanja in uporabo v različnih panogah. V nadaljnje smo opisali imobilizacijo na magnetne nanodelce (MNP), pri čemer smo se osredotočili na AMN-MNPs. Podan je tudi pregled literature o imobilizaciji l-ASNaze na MNPs. Pri eksperimentalnem delu smo proučevali vpliv različnih parametrov, kot so koncentracija mrežnega povezovalca glutaraldehida (GA), vrtilna hitrost, čas in temperatura imobilizacije, z namenom doseganje čim višje aktivnosti imobiliziranega encima in učinkovitost imobilizacije. Zanimalo nas je kakšno aktivnost encima dosežemo ob dodatku ogrodnih proteinov, ki delujejo kot stabilizatorji. Uporabili smo goveji serumski albumin (BSA) in albumin iz jajčnih beljakov (EA). V nadaljnje smo proučili termično stabilnost proste in imobilizirane l-ASNaze pri različnih časih inkubacije in pri različnih temperaturah. Prosto in imobilizirano l-ASNazo smo vzpostavili na magnetno polje in primerjali aktivnosti l-ASNaze pred in po vzpostavitvi.
Keywords:l-asparaginaza, magnetni nanodelci, stabilnost, kovalentna vezava, funkcionalizacija, imobilizacija
Place of publishing:Maribor
Place of performance:Maribor
Publisher:[M. Verdev]
Year of publishing:2024
Number of pages:1 spletni vir (1 datoteka PDF (X, 41 f.))
PID:20.500.12556/DKUM-90497 New window
UDC:577.151:544.142.2(043.2)
COBISS.SI-ID:212127235 New window
Publication date in DKUM:02.10.2024
Views:0
Downloads:33
Metadata:XML DC-XML DC-RDF
Categories:KTFMB - FKKT
:
Copy citation
  
Average score:(0 votes)
Your score:Voting is allowed only for logged in users.
Share:Bookmark and Share


Hover the mouse pointer over a document title to show the abstract or click on the title to get all document metadata.

Licences

License:CC BY 4.0, Creative Commons Attribution 4.0 International
Link:http://creativecommons.org/licenses/by/4.0/
Description:This is the standard Creative Commons license that gives others maximum freedom to do what they want with the work as long as they credit the author.
Licensing start date:06.09.2024

Secondary language

Language:English
Title:Immobilization of l-asparaginase on magnetic nanoparticles
Abstract:As part of the final work, we performed optimization of the immobilization of the enzyme L-asparaginase (ASNase) on aminosilane magnetic nanoparticles (AMN-MNPs). The immobilization process consists of two steps, AMN-MNPs functionalization and enzyme immobilization. In the first step, AMN-MNPs were functionalized, and in the second step, ASNase was immobilized on them. First, in the theoretical part, we described the properties of ASNase, showed its structure, mechanism of function and use in various branches. We further described the immobilization on magnetic nanoparticles (MNPs), focusing on AMN-MNPs. A literature review on the immobilization of ASNase on MNPs is also given. In the experimental work, we studied the influence of various parameters, such as the concentration of the crosslinker glutaraldehyde (GA), rotation speed, time and temperature of immobilization, with the aim of achieving the highest possible activity of the immobilized enzyme and immobilization efficiency. We were interested in what kind of enzyme activity is achieved with the addition of framework proteins that act as stabilizers. Bovine serum albumin (BSA) and egg white albumin (EA) were used. We further studied the thermal stability of free and immobilized ASNase at different incubation times and at different temperatures. Free and immobilized ASNase were exposed to a magnetic field and ASNase activities were compared before and after exposure. The final work contains a discussion of the results and graphically displayed results.
Keywords:L-asparaginase, magnetic nanoparticles, stability, covalent binding, functionalization, immobilization


Comments

Leave comment

You must log in to leave a comment.

Comments (0)
0 - 0 / 0
 
There are no comments!

Back
Logos of partners University of Maribor University of Ljubljana University of Primorska University of Nova Gorica