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master's thesis
Računalna i eksperimentalna karakterizacija esteraze iz Rhodopseudomonas Palustris za razgradnju polimliječne kiseline
Zagreb: University of Zagreb, Faculty of Science, 2024. urn:nbn:hr:217:245970
Mendeš, Davor
University of Zagreb
Faculty of Science
Department of Chemistry

Institutional repository: Repository of the Faculty of Science

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Mendeš, D. (2024). Računalna i eksperimentalna karakterizacija esteraze iz Rhodopseudomonas Palustris za razgradnju polimliječne kiseline (Master's thesis). Zagreb: University of Zagreb, Faculty of Science. Retrieved from https://urn.nsk.hr/urn:nbn:hr:217:245970

Mendeš, Davor. "Računalna i eksperimentalna karakterizacija esteraze iz Rhodopseudomonas Palustris za razgradnju polimliječne kiseline." Master's thesis, University of Zagreb, Faculty of Science, 2024. https://urn.nsk.hr/urn:nbn:hr:217:245970

Mendeš, Davor. "Računalna i eksperimentalna karakterizacija esteraze iz Rhodopseudomonas Palustris za razgradnju polimliječne kiseline." Master's thesis, University of Zagreb, Faculty of Science, 2024. https://urn.nsk.hr/urn:nbn:hr:217:245970

Mendeš, D. (2024). 'Računalna i eksperimentalna karakterizacija esteraze iz Rhodopseudomonas Palustris za razgradnju polimliječne kiseline', Master's thesis, University of Zagreb, Faculty of Science, accessed 04 November 2024, https://urn.nsk.hr/urn:nbn:hr:217:245970

Mendeš D. Računalna i eksperimentalna karakterizacija esteraze iz Rhodopseudomonas Palustris za razgradnju polimliječne kiseline [Master's thesis]. Zagreb: University of Zagreb, Faculty of Science; 2024 [cited 2024 November 04] Available at: https://urn.nsk.hr/urn:nbn:hr:217:245970

D. Mendeš, "Računalna i eksperimentalna karakterizacija esteraze iz Rhodopseudomonas Palustris za razgradnju polimliječne kiseline", Master's thesis, University of Zagreb, Faculty of Science, Zagreb, 2024. Available at: https://urn.nsk.hr/urn:nbn:hr:217:245970

Metadata
TitleRačunalna i eksperimentalna karakterizacija esteraze iz Rhodopseudomonas Palustris za razgradnju polimliječne kiseline
Title (english)Computational and experimental characterization of esterase from Rhodopseudomons palustris for the degradation of polylactic acid
AuthorDavor Mendeš
MentorAleksandra Maršavelski (mentor)
MentorMarko Močibob (mentor)
Committee memberAleksandra Maršavelski (predsjednik povjerenstva)
Committee memberMarko Močibob (član povjerenstva)
Committee memberIvan Kodrin (član povjerenstva)
Committee memberTomica Hrenar (član povjerenstva)
Committee memberĐani Škalamera (član povjerenstva)
GranterUniversity of Zagreb
Faculty of Science
(Department of Chemistry)
Zagreb
Defense date and country2024-02-23, Croatia
Scientific / art field,
discipline and subdiscipline		NATURAL SCIENCES
Chemistry
Abstract
U sklopu diplomskog rada okarakterizirana je α/β hidrolaza RPA1511 iz bakterije Rhodopseudomonas palustris s hidrolitičkom aktivnosti prema polimliječnoj kiselini. Konstruirana je mutirana inačica Arg243Lys, a konstrukcija mutanta motivirana je prethodnim in silico istraživanjem. Hidrolaze su heterologno eksprimirane u bakteriji Escherichia coli, potom su eksprimirani proteini pročišćeni afinitetnom kromatografijom. Aktivnost hidrolize hidrolaza polimliječne kiseline ispitana je na suspenziji polimliječne kiseline uklopljene u agarozi te pomoću turbidimetrijskog testa. Dinamika RPA1511 i njene mutirane inačice ispitana je pomoću simulacija molekularne dinamike, te je procijenjena entalpija vezanja modelnog supstrata dekamera mliječne kiseline. Nadalje, istražen je pojedinačni doprinos aminokiselina entalpije vezanja dekamera mliječne kiseline.
Abstract (english)
In this work, an α/β hydrolase RPA1511 from Rhodopseudomonas palustris with activity towards polylactic acid was characterized experimentally and computationally by means of turibidmetric assays and molecular dynamics simulations. Motivated by in silico studies perfomed on RPA1511, a mutant Arg243Lys with potentially higher hydrolitic acitvity towards polylactic acid was also characterized. Both hydrolazes were expressed heterologously in Escherichia coli and purified by affinity chromatography. Their hydrolitic acitivity towards polylactic acid was assessed on polyester suspension solidified with agarose and by turbidimetric suspension assay. On the other hand, their dynamical properties were studied in silico utilizing molecular dynamics simulations modelled with the decamer of lactic acid. The binding enthalpy was calculated with the use of an end-point method. To assess the importance of amino acid residues involved in binding decameric lactic acid, the per-residue enthalpy decomposition was calculated.
Keywords
Keywords (english)
Languagecroatian
URN:NBNurn:nbn:hr:217:245970
Study programmeTitle: Graduate university studies in chemistry; specializations in: Graduate university studies in chemistry
Course: Graduate university studies in chemistry
Study programme type: university
Study level: graduate
Academic / professional title: sveučilišni/a magistar/magistra kemije (sveučilišni/a magistar/magistra kemije)
Type of resourceText
File originBorn digital
Access conditionsOpen access
Terms of useLicence In copyright icon
Created on2024-03-08 09:16:49