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Title:
Imobilizacija lakaze v zamrežene encimske skupke (CLEAs)
Authors:
ID
Petek, Mihaela
(Author)
ID
Leitgeb, Maja
(Mentor)
More about this mentor...
ID
Vasić, Katja
(Comentor)
Files:
UN_Petek_Mihaela_2017.pdf
(1,71 MB)
MD5: 63DF079D0DE232015B048FE5E389102D
PID:
20.500.12556/dkum/9764e1a9-ef88-4904-87ab-803588f7ffb2
Language:
Slovenian
Work type:
Bachelor thesis/paper
Typology:
2.11 - Undergraduate Thesis
Organization:
FKKT - Faculty of Chemistry and Chemical Engineering
Abstract:
Diplomsko delo opisuje sintezo zamreženih encimskih skupkov iz encima lakaze (CLEAs). Sinteza CLEAs delcev iz lakaze je potekala po določenem postopku, pri katerem sta najpomembnejši fazi obarjanje in zamreženje. Raztopino encima lakaze smo obarjali v različnih obarjalnih reagentih, najuspešnejša sta bila obarjalna reagenta etanol, 1-propanol in 2-propanol. Oborjeni encim smo zamreževali z mrežnim povezovalcem glutaraldehidom. Zamreženim encimskim skupkom smo določevali učinkovitost imobilizacije in preostalo aktivnost imobiliziranega encima v primerjavi s prostim encimom. Pri postopku imobilizacije smo z namenom, da bi dosegli čim višjo učinkovitost imobilizacije ter čim višjo preostalo aktivnost imobiliziranega encima, spreminjali parametre, kot so volumski deleži glutaraldehida, čas zamreženja, vpliv ogrodnih proteinov govejega seruma albumina (BSA) in jajčnega albumina (EA), volumski deleži natrijevega cianoborohidrida in temperaturo zamreženja. Vse vzorce smo tudi dvakrat spirali, z namenom da bi odstranili nezamrežen encim.
Keywords:
Lakaza
,
imobilizacija
,
zamreženi encimski skupki
,
obarjanje
,
zamreženje
,
glutaraldehid
,
encimska aktivnost
Place of publishing:
Maribor
Publisher:
[M. Petek]
Year of publishing:
2017
PID:
20.500.12556/DKUM-68276
UDC:
544.478.3(043.2)
COBISS.SI-ID:
21062166
NUK URN:
URN:SI:UM:DK:JVMQ3FEQ
Publication date in DKUM:
22.11.2017
Views:
1868
Downloads:
168
Metadata:
Categories:
KTFMB - FKKT
Cite this work
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:
PETEK, Mihaela, 2017,
Imobilizacija lakaze v zamrežene encimske skupke (CLEAs)
[online]. Bachelor’s thesis. Maribor : M. Petek. [Accessed 21 January 2025]. Retrieved from: https://dk.um.si/IzpisGradiva.php?lang=eng&id=68276
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Licences
License:
CC BY 4.0, Creative Commons Attribution 4.0 International
Link:
http://creativecommons.org/licenses/by/4.0/
Description:
This is the standard Creative Commons license that gives others maximum freedom to do what they want with the work as long as they credit the author.
Licensing start date:
14.09.2017
Secondary language
Language:
English
Title:
Immobilization of laccase in the cross-linked enzyme aggregates (CLEAs)
Abstract:
The diploma work describes synthesis of cross-linked enzyme aggregates (CLEAs) of laccase enzyme. Synthesis of CLEAs laccase was carried out according to a particular process in which percipitation and cross-linking are the most important stages. The solution of the laccase enzyme was precipitated in various precipitation reagents, the most successful were ethanol, 1-propanol and 2-propanol. The precipitated enzyme was cross-linked with the cross-linker glutaraldehyde. The immobilization efficiency and the residual specific activity of immobilized enzyme as cross-linked enzyme aggregates was determined in comparison with free enzyme. Parameters, such as volume fraction of glutaraldehyde, cross-linking time, influence of stability proteins bovine serum albumin (BSA) and egg albumin (EA), volume fraction of sodium cyanoborohydride and the temperature of cross-linking, have been optimized to achieve the highest immobilization efficiency and the highest residual specific activity of the cross-linked enzyme. All the samples were also washed two times to remove the noncross-linked enzyme.
Keywords:
Laccase
,
immobilization
,
cross-linked enzyme aggregates
,
precipitation
,
cross-linking
,
glutaraldehyde
,
enzyme activity
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