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Title:
Imobilizacija ß-laktamaze : magistrsko delo
Authors:
ID
Brumen, Adam
(Author)
ID
Leitgeb, Maja
(Mentor)
More about this mentor...
ID
Primožič, Mateja
(Comentor)
ID
Vasić, Katja
(Comentor)
Files:
MAG_Brumen_Adam_2023.pdf
(2,32 MB)
MD5: EEE55795671FF698DB6F2695B0D41D39
Language:
Slovenian
Work type:
Master's thesis/paper
Typology:
2.09 - Master's Thesis
Organization:
FKKT - Faculty of Chemistry and Chemical Engineering
Abstract:
Namen magistrskega dela je predstaviti pomen encima β-laktamaze za javno zdravje, kemijske in fizikalne metode imobilizacije encimov ter magnetne nanodelce kot nosilce za imobilizacijo encimov. V okviru naloge smo izvedli imobilizacijo β-laktamaze na magnetne nanodelce, ki se lahko uporablja za razgradnjo antibiotikov. β-Laktamaza razgrajuje antibiotike z β-laktamskimi obroči, natančneje peniciline, cefalosporine in karbapeneme. V okviru raziskovalnega dela smo uspešno sintetizirali aminosilanske magnetne nanodelce, ki smo jih uporabili za imobilizacijo encima. Z dodajanjem mrežnih povezovalcev in stabilizacijskih proteinov ter s spreminjanjem sinteznih parametrov, kot so temperatura, pH, vrtilna hitrost in čas imobilizacije, smo določili optimalne parametre za imobilizacijo obravnavanega encima na magnetne nanodelce. Pri raziskovalnem delu smo tako uporabili 20 mg aminosilanskih nanodelcev in encim β-laktamazo s koncentracijo 0,01 mg/mL. Ugotovili smo, da je optimalen dodatek mrežnega povezovalca glutaraldehida 10 % (v/v), optimalen dodatek govejega seruma albumina 25 % (v/v), vrtilna hitrost 450 rpm in čas imobilizacije dve uri. Proučevali smo tudi stabilnost prostega in imobiliziranega encima. Izvedli smo tudi študijo večkratne uporabe imobiliziranega encima. Po petnajstih ciklih ponovne uporabe je imobilizirani encim ohranil 12,3 % svoje začetne aktivnosti.
Keywords:
imobilizacija encima
,
magnetni nanodelci
,
β-laktamaza
,
β-laktamski antibiotiki
,
mrežni povezovalec
Place of publishing:
Maribor
Place of performance:
Maribor
Publisher:
[A. Brumen]
Year of publishing:
2023
Number of pages:
1 spletni vir (1 datoteka PDF (X, 41 f.))
PID:
20.500.12556/DKUM-85963
UDC:
534.645.4(043.2)
COBISS.SI-ID:
171619331
Publication date in DKUM:
10.10.2023
Views:
497
Downloads:
137
Metadata:
Categories:
KTFMB - FKKT
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:
BRUMEN, Adam, 2023,
Imobilizacija ß-laktamaze : magistrsko delo
[online]. Master’s thesis. Maribor : A. Brumen. [Accessed 11 April 2025]. Retrieved from: https://dk.um.si/IzpisGradiva.php?lang=eng&id=85963
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Licences
License:
CC BY-NC-ND 4.0, Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International
Link:
http://creativecommons.org/licenses/by-nc-nd/4.0/
Description:
The most restrictive Creative Commons license. This only allows people to download and share the work for no commercial gain and for no other purposes.
Licensing start date:
22.09.2023
Secondary language
Language:
English
Title:
Imobilization of ß-lactamase
Abstract:
The purpose of the master's thesis is to present the importance of the β-lactamase enzyme to public health, chemical and physical methods of enzyme immobilization, and magnetic nanoparticles as carriers for immobilization. For immobilization, we used the enzyme β-lactamase, which degrades antibiotics with β-lactam rings, specifically penicillins, cephalosporins and carbapenems, and therefore represents one of the major clinical problems. As part of the research work, we successfully synthesized maghemite aminosilane nanoparticles, which were used for enzyme immobilization. By adding network linkers and stabilizing proteins and by changing parameters such as temperature, pH, rotation speed and immobilization time, we determined the optimal parameters for the immobilization of the enzyme in question on magnetic nanoparticles. In the research work, we used 20 mg of aminosilane nanoparticles and the enzyme β-lactamase with the conentration of 0,01 mg/mL and found that that the optimal addition of the crosslinker glutaraldehyde is 10% (v/v), the optimal addition of bovine serum albumin is 25% (v/v), the rotation speed is 450 rpm and the immobilization time is two hours. Incubation caused a steep drop in the residual activity of the free enzyme over time, while the activity of the immobilized enzyme was almost completely preserved. After fifteen cycles of use, the immobilized enzyme retained 12.3 percent of the activity compared to the immobilized enzyme at the first use and 14 percent compared to the free enzyme at the first use.
Keywords:
enzyme immobilization
,
magnetic nanoparticles
,
β-lactamase
,
β-lactam antibiotics
,
cross-linking agent
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