| | SLO | ENG | Cookies and privacy

Bigger font | Smaller font
First page > Show document

Show document Help

Title:OPTIMIZACIJA PARAMETROV ZA SINTEZO ZAMREŽENIH ENCIMSKIH SKUPKOV IZ ENCIMA HOLESTEROL OKSIDAZE
Authors:ID Smrečnjak, Nataša (Author)
ID Leitgeb, Maja (Mentor) More about this mentor... New window
ID Primožič, Mateja (Comentor)
Files:.pdf VS_Smrecnjak_Natasa_2011.pdf (2,40 MB)
MD5: 04D920014A7038F8FC0D15266127FFAE
PID: 20.500.12556/dkum/39f64a42-c199-41a5-909d-c39020a99bc7
 
Language:Slovenian
Work type:Undergraduate thesis
Organization:FKKT - Faculty of Chemistry and Chemical Engineering
Abstract:Delo opisuje optimizacijo ključnih parametrov za sintezo katalitično aktivnih zamreženih encimskih skupkov (CLEAs) iz holesterol oksidaze (ChOx, EC 1.1.3.6). Optimizacija reakcijskih parametrov za sintezo CLEAs je obsegala iskanje optimalnega obarjalnega reagenta, optimalne koncentracije mrežnega povezovalca, optimalne koncentracije biokatalizatorja ChOx ter optimalnega koncentracijskega razmerja med holesterol oksidazo in inertnim proteinom albuminom iz kokošjih jajc (Egg albumin, EA). Sinteza zamreženih encimskih skupkov je bila razdeljena na dva ključna dela; na obarjanje topnega oziroma nativnega biokatalizatorja z ustreznim organskim topilom in na zamreženje tako izoborjenega biokatalizatorja s pomočjo mrežnega povezovalca. V našem primeru smo uspešno sintetizirali zamrežene encimske skupke iz holesterol oksidaze. Aktivnost zamreženih encimskih skupkov smo določili z reakcijo oksidacije holesterola. Optimalni reakcijski pogoji sinteze zamreženih encimskih skupkov so bili doseženi pri koncentraciji encima ChOx 2 mg/mL in koncentraciji ogrodnega proteina albumina 2 mg/mL. Ugotovili smo, da je bila aktivnost zamreženih encimskih skupkov iz biokatalizatorja holesterol oksidaze najvišja pri koncentraciji glutaraldehida 1,8 % (v/v) in acetonu kot obarjalnemu reagentu. Končna aktivnost CLEAs iz holesterol oksidaze pri optimalnih reakcijskih pogojih je bila 94 %.
Keywords:zamreženi encimski skupki, imobilizacija, holesterol oksidaza, optimizacija, reakcijski parametri
Place of publishing:Maribor
Publisher:[N. Smrečnjak]
Year of publishing:2011
PID:20.500.12556/DKUM-17256 New window
UDC:547.914+577.17(043.2)
COBISS.SI-ID:14932502 New window
NUK URN:URN:SI:UM:DK:KC7AOLKX
Publication date in DKUM:19.01.2011
Views:3262
Downloads:242
Metadata:XML DC-XML DC-RDF
Categories:KTFMB - FKKT
:
SMREČNJAK, Nataša, 2011, OPTIMIZACIJA PARAMETROV ZA SINTEZO ZAMREŽENIH ENCIMSKIH SKUPKOV IZ ENCIMA HOLESTEROL OKSIDAZE [online]. Bachelor’s thesis. Maribor : N. Smrečnjak. [Accessed 5 May 2025]. Retrieved from: https://dk.um.si/IzpisGradiva.php?lang=eng&id=17256
Copy citation
  
Average score:
0.5
1
1.5
2
2.5
3
3.5
4
4.5
5
(0 votes)
Your score:Voting is allowed only for logged in users.
Share:Bookmark and Share


Searching for similar works...Please wait....
Hover the mouse pointer over a document title to show the abstract or click on the title to get all document metadata.

Secondary language

Language:English
Title:OPTIMIZATION OF PARAMETERS FOR SYNTHESIS OF CROSS-LINKED ENZYME CLUSTERS FROM CHOLESTEROL OXIDASE
Abstract:The study describes optimization of the key parameters for the synthesis of catalytically-active cross-linked enzyme aggregates (CLEAs), made of cholesterol oxidase (ChOx, EC 1.1.3.6). The optimization of the reaction parameters consists of seeking for the best precipitant, for the optimal concentration of the cross-linker, for the optimal enzyme concentration and for the optimal concentration ratio betwen cholesterol oxidase and inert protein albumin from chicken eggs (Egg albumin, EA). The synthesis of cross-linked enzyme aggregates was divided into two main parts; the precipitation of soluble or native enzyme with a suitable organic solvent and cross-linking of enzyme aggregates with the help of a cross-linker. Cross-linked cholesterol oxidase enzyme aggregates, which activity was determined by the reaction of oxidation of cholesterol who successfully synthesized. Optimal reaction conditions for CLEAs preparation were found at ChOx enzyme concentration of 2 mg/mL and the albumin concentration of 2 mg/mL. The higest activity recovery of CLEAs was obtained at glutaraldehyde concentracion 1,8 % (v/v) and when the acetone as a precipitant of choice was used. The final activity of CLEAs of cholesterol oxidase, achieved at the optimal reaction conditions, was 94 %.
Keywords:cross-linked enzyme aggregates, immobilization, cholesterol oxidase, optimization, reaction parameters


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