Imobilizacija lakaze v zamrežene encimske skupke (CLEAs)

diplomsko delo univerzitetnega študijskega programa I. stopnje

Mihaela Petek (Author), Maja Leitgeb (Mentor), Katja Heržič (Co-mentor)

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;diplomske naloge;

Data

Language:	Slovenian
Year of publishing:	2017
Typology:	2.11 - Undergraduate Thesis
Organization:	UM FKKT - Faculty of Chemistry and Chemical Engineering
Publisher:	[M. Petek]
UDC:	544.478.3(043.2)
COBISS:	21062166
Views:	1182
Downloads:	147
Average score:	0 (0 votes)
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Other data

Secondary language:	English
Secondary title:	Immobilization of laccase in the cross-linked enzyme aggregates (CLEAs)
Secondary 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.
Secondary keywords:	laccase;immobilization;crocross-linked enzyme aggregates;precipitation;cross-linking;glutaraldehyde;enzyme activity;
URN:	URN:SI:UM:
Type (COBISS):	Bachelor thesis/paper
Thesis comment:	Univ. v Mariboru, Fak. za kemijo in kemijsko tehnologijo
Pages:	IX, 44 f.
ID:	10864308