prikaz prve stranice dokumenta Primjena metagenomskih esteraza za okolišno prihvatljivu razgradnju polimliječne kiseline
Embargo period 2025-02-21
master's thesis
Primjena metagenomskih esteraza za okolišno prihvatljivu razgradnju polimliječne kiseline
Zagreb: University of Zagreb, Faculty of Science, 2024. urn:nbn:hr:217:597947
Josić, Eva
University of Zagreb
Faculty of Science
Department of Chemistry

Institutional repository: Repository of the Faculty of Science

Cite this document

Josić, E. (2024). Primjena metagenomskih esteraza za okolišno prihvatljivu razgradnju polimliječne kiseline (Master's thesis). Zagreb: University of Zagreb, Faculty of Science. Retrieved from https://urn.nsk.hr/urn:nbn:hr:217:597947

Josić, Eva. "Primjena metagenomskih esteraza za okolišno prihvatljivu razgradnju polimliječne kiseline." Master's thesis, University of Zagreb, Faculty of Science, 2024. https://urn.nsk.hr/urn:nbn:hr:217:597947

Josić, Eva. "Primjena metagenomskih esteraza za okolišno prihvatljivu razgradnju polimliječne kiseline." Master's thesis, University of Zagreb, Faculty of Science, 2024. https://urn.nsk.hr/urn:nbn:hr:217:597947

Josić, E. (2024). 'Primjena metagenomskih esteraza za okolišno prihvatljivu razgradnju polimliječne kiseline', Master's thesis, University of Zagreb, Faculty of Science, accessed 29 December 2024, https://urn.nsk.hr/urn:nbn:hr:217:597947

Josić E. Primjena metagenomskih esteraza za okolišno prihvatljivu razgradnju polimliječne kiseline [Master's thesis]. Zagreb: University of Zagreb, Faculty of Science; 2024 [cited 2024 December 29] Available at: https://urn.nsk.hr/urn:nbn:hr:217:597947

E. Josić, "Primjena metagenomskih esteraza za okolišno prihvatljivu razgradnju polimliječne kiseline", Master's thesis, University of Zagreb, Faculty of Science, Zagreb, 2024. Available at: https://urn.nsk.hr/urn:nbn:hr:217:597947

Metadata
TitlePrimjena metagenomskih esteraza za okolišno prihvatljivu razgradnju polimliječne kiseline
Title (english)Application of metagenomic esterases for environmentally friendly degradation of polylactic acid
AuthorEva Josić
MentorAleksandra Maršavelski (mentor)
MentorMarko Močibob (mentor)
Committee memberAleksandra Maršavelski (predsjednik povjerenstva)
Committee memberTajana Begović (član povjerenstva)
Committee memberIvana Kekez (član povjerenstva)
Committee memberMarko Močibob (član povjerenstva)
GranterUniversity of Zagreb
Faculty of Science
(Department of Chemistry)
Zagreb
Defense date and country2024-02-21, Croatia
Scientific / art field,
discipline and subdiscipline		NATURAL SCIENCES
Chemistry
Abstract
Polimliječna kiselina (PLA) je biorazgradiv polimer čija su termička i mehanička obilježja slična masovno korištenoj plastici problematičnoj za zbrinjavanje. Biorazgradivosti i fizikalna svojstva čine PLA kandidatom za proizvodnju plastike koja se može razgraditi na okolišno prihvatljiv način. Enzimi koji razgrađuju PLA, za prihvatljivu okolišnu i industrijsku razgradnju, spadaju u skupinu α/β-hidrolaza. Trenutno je identificiran mali broj hidrolaza s aktivnošću prema PLA, a jednu od najvećih posjeduje nedavno otkriveni enzim MGS0156. U ovom diplomskom radu proizvedeni su MGS0156, njegov mutant i novi, do sada neokarakterizirani homolog, pronađen pretragom metagenomskih baza podataka. Hidrolitička aktivnost enzima prema PLA provjerena je u agaroznom gelu i slobodnoj suspenziji. Ovdje je prvi put pokazana aktivnost novog metagenomskog enzima prema PLA, koja se pokazala značajno većom od većine aktivnosti zabilježenih u literaturi. Računalnim metodama utvrđeno je da oba enzima imaju mobilni poklopac, identificirane su aminokiseline veznog mjesta s najvećim doprinosom vezanju supstrata i potencijalne mete za mutacije.
Abstract (english)
Polylactic acid (PLA) is a biodegradable polymer with thermal and mechanical properties like those of widely used plastics with problematic disposal. Its biodegradability and physical properties make PLA a candidate for environmentally friendly plastic production. PLA-degrading enzymes used for environmentally friendly and industrial degradation, belong to the α/β-hydrolase group. A small number of PLA-hydrolases is identified, with one of the greatest activities belonging to a recently discovered MGS0156. Here, MGS0156, its mutant and a new, previously uncharacterized homologue discovered in metagenomic databases were produced. The hydrolytic activity towards PLA was tested in an agarose gel and a suspension. The hydrolytic activity of the new metagenomic enzyme was demonstrated for the first time and was found to be significantly higher than most activities documented in the literature. Using computational methods, it was found that both enzymes contain a mobile lid, binding site amino acids with the largest contribution to substrate binding were identified as well as potential mutation targets
Keywords
Keywords (english)
Languagecroatian
URN:NBNurn:nbn:hr:217:597947
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 conditionsEmbargoed access
Embargo expiration date: 2025-02-21
Terms of useLicence In copyright icon
Created on2024-03-07 14:14:31