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undergraduate thesis
Praćenje stabilnosti enzima putem mjerenja raspodjele veličine proteina
Zagreb: University of Zagreb, Faculty of Chemical Engineering and Technology, 2022. urn:nbn:hr:149:486322
Arambašić, Barbara
University of Zagreb
Faculty of Chemical Engineering and Technology

Institutional repository: Repository of Faculty of Chemical Engineering and Technology University of Zagreb

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Arambašić, B. (2022). Praćenje stabilnosti enzima putem mjerenja raspodjele veličine proteina (Undergraduate thesis). Zagreb: University of Zagreb, Faculty of Chemical Engineering and Technology. Retrieved from https://urn.nsk.hr/urn:nbn:hr:149:486322

Arambašić, Barbara. "Praćenje stabilnosti enzima putem mjerenja raspodjele veličine proteina." Undergraduate thesis, University of Zagreb, Faculty of Chemical Engineering and Technology, 2022. https://urn.nsk.hr/urn:nbn:hr:149:486322

Arambašić, Barbara. "Praćenje stabilnosti enzima putem mjerenja raspodjele veličine proteina." Undergraduate thesis, University of Zagreb, Faculty of Chemical Engineering and Technology, 2022. https://urn.nsk.hr/urn:nbn:hr:149:486322

Arambašić, B. (2022). 'Praćenje stabilnosti enzima putem mjerenja raspodjele veličine proteina', Undergraduate thesis, University of Zagreb, Faculty of Chemical Engineering and Technology, accessed 26 December 2024, https://urn.nsk.hr/urn:nbn:hr:149:486322

Arambašić B. Praćenje stabilnosti enzima putem mjerenja raspodjele veličine proteina [Undergraduate thesis]. Zagreb: University of Zagreb, Faculty of Chemical Engineering and Technology; 2022 [cited 2024 December 26] Available at: https://urn.nsk.hr/urn:nbn:hr:149:486322

B. Arambašić, "Praćenje stabilnosti enzima putem mjerenja raspodjele veličine proteina", Undergraduate thesis, University of Zagreb, Faculty of Chemical Engineering and Technology, Zagreb, 2022. Available at: https://urn.nsk.hr/urn:nbn:hr:149:486322

Metadata
TitlePraćenje stabilnosti enzima putem mjerenja raspodjele veličine proteina
Title (english)Monitoring of enzyme stability by measuring protein size distribution
AuthorBarbara Arambašić
MentorZvjezdana Findrik Blažević (mentor)
Committee memberZvjezdana Findrik Blažević (predsjednik povjerenstva)
Committee memberMarija Vuković Domanovac (član povjerenstva)
Committee memberMiroslav Jerković (član povjerenstva)
GranterUniversity of Zagreb
Faculty of Chemical Engineering and Technology
Zagreb
Defense date and country2022-09-19, Croatia
Scientific / art field,
discipline and subdiscipline		TECHNICAL SCIENCES
Chemical Engineering
Abstract
N-acetilneuraminska kiselina (Neu5Ac) je sijalična kiselina čiju sintezu katalizira enzim N-acetilneuraminat sintaza. N-acetilmanozamin (MaNAc) kondenzacijom s fosfoenolpiruvatom (PEP) daje N-acetilneuraminsku kiselinu (Neu5Ac). Za potrebe ovog rada enzim je pripremljen i pročišćen. Prekomjerna ekspresija proteina neuB, koji kodira N-acetilneuraminat sintazu, postignuta je ubacivanjem plazmida u genetski modificirane stanice Escherichia coli. Bakterijske stanice razbijene su ultrazvukom i pročišćene centrifugiranjem. Dobiveni enzim pročišćen je u koloni s niklom i nitrilotrioctenom kiselinom i skladišten u odgovarajućem puferu na 4°C. Stabilnost enzima sintaze N-acetilneuraminske kiseline (NeuS) je praćena preko specifične aktivnosti, raspodjele veličina čestica i koncentracije proteina.
Abstract (english)
N-acetylneuraminic acid (Neu5Ac) is a sialic acid whose synthesis is catalyzed by the enzyme N-acetylneuramine synthase. N-acetylmannosamine (MaNAc) by condensation with phosphoenolpyruvate (PEP) gives N-acetylneuraminic acid (Neu5Ac). For the purposes of this work the enzyme was prepared and purified. Overexpression of the protein neuB, which encodes N-acetylneuramine synthase, was achieved by inserting the plasmid into genetically modified Escherichia coli cells. Bacterial cells were disrupted by ultrasound and purified by centrifugation. The resulting enzyme was purified in a column with nickel and nitrilotriooctenoic acid and stored in the appropriate buffer at 4°C. The stability of N-acetylneuraminate synthase (NeuS) enzyme was monitored through specific activity, particle size distribution and protein concentration.
Keywords
Keywords (english)
Languagecroatian
URN:NBNurn:nbn:hr:149:486322
ProjectNumber: 956631
Title: C-C Bond Formation Using Top Performing Enzymes
Acronym: CC-Top
Leader: Zvjezdana Findrik Blažević
Jurisdiction: eu
Funder: EK
Funding stream: H2020
Study programmeTitle: Chemical Engineering - Undergraduate study
Study programme type: university
Study level: undergraduate
Academic / professional title: sveučilišni/a prvostupnik/ prvostupnica (baccalaureus/baccalaurea) inženjer/inženjerka kemijskog inženjerstva (sveučilišni/a prvostupnik/ prvostupnica (baccalaureus/baccalaurea) inženjer/inženjerka kemijskog inženjerstva)
Type of resourceText
File originBorn digital
Access conditionsOpen access
Embargo expiration date: 2023-09-19
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Created on2023-02-17 13:22:46