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Title:IMOBILIZACIJA HRENOVE PEROKSIDAZE NA MAGHEMITNE NANODELCE, MODIFICIRANE Z AMINOSILANOM IN HITOZANOM
Authors:ID Pezdevšek, Nataša (Author)
ID Leitgeb, Maja (Mentor) More about this mentor... New window
ID Primožič, Mateja (Comentor)
Files:.pdf UNI_Pezdevsek_Natasa_2012.pdf (10,07 MB)
MD5: 68E11F1DE63ADBE634D226FD6EDE926B
PID: 20.500.12556/dkum/6b01f2cb-1f53-45a2-8b02-77e003cee763
 
Language:Slovenian
Work type:Undergraduate thesis
Typology:2.11 - Undergraduate Thesis
Organization:FKKT - Faculty of Chemistry and Chemical Engineering
Abstract:Namen diplomske naloge je optimizacija procesnih pogojev za imobilizacijo encima hrenove peroksidaze na površinsko modificirane maghemitne nanodelce. Spreminjali smo masno razmerje med nosilcem in encimom, koncentracijo mrežnega povezovalca glutaraldehida in čas imobilizacije. Primerjali smo učinkovitost imobilizacije ter ohranjeno aktivnost encima, vezanega na aminosilanske in hitozanske maghemitne nanodelce. Maghemitne nanodelce smo sintetizirali s koprecipitacijo Fe2+ in Fe3+ ionov ob dodatku obarjalnega reagenta, 25 % amonijaka. Aminosilanske maghemitne nanodelce smo pripravili v dveh stopnjah. Najprej smo nanodelce prevlekli s funkcionalno plastjo silike (SiO2), nato pa še s plastjo aminosilana. Hitozanski maghemitni nanodelci so bili pripravljeni po treh različnih postopkih. Kljub dobri učinkovitosti imobilizacije, se v nobenem primeru ni ohranila visoka aktivnost encima. Najvišjo ohranjeno aktivnost imobiliziranega encima smo dosegli pri aminosilanskih nanodelcih, in sicer 2,06 % pri 65,76 % učinkovitosti imobilizacije. Prav tako je imobiliziran encim v primerjavi s prostim encimom pokazal nižjo stabilnost pri povišanem tlaku in temperaturi. Z zvišanjem temperature pri atmosferskem tlaku, se je aktivnost prostega in imobiliziranega encima izboljšala.
Keywords:Imobilizacija encima, hrenova peroksidaza, maghemitni nanodelci, aminosilanski maghemitni nanodelci, hitozanski maghemitni nanodelci, učinkovitost imobilizacije, aktivnost encima
Place of publishing:Maribor
Publisher:[N. Pezdevšek]
Year of publishing:2012
PID:20.500.12556/DKUM-38597 New window
UDC:579.22(043.2)
COBISS.SI-ID:16704278 New window
NUK URN:URN:SI:UM:DK:FP1TUWVG
Publication date in DKUM:16.10.2012
Views:2780
Downloads:390
Metadata:XML RDF-CHPDL DC-XML DC-RDF
Categories:KTFMB - FKKT
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Secondary language

Language:English
Title:IMMOBILIZATION OF HORSERADISH PEROXIDASE ONTO MAGHEMITE NANOPARTICLES, MODIFIED WITH AMINOSILANE AND CHITOSAN
Abstract:The purpose of the diploma thesis is optimization of process conditions for immobilization of horseradish peroxidase onto surface modified maghemite nanoparticles. By varying the mass ratio between carrier and enzyme, concentration of glutaraldehyde and duration time of immobilization, the comparison of the binding efficiency and residual activity of enzyme, immobilized onto maghemite nanoparticles coated by aminosilane and chitosan was done. Maghemite nanoparticles were synthetized by coprecipitation of Fe2+ and Fe3+ ions by adding an 25 % ammonia as precipitation agent. Aminosilane coated maghemite nanoparticles were prepared in two stages. First, maghemite nanoparticles were functionalized with silica (SiO2) and afterwards with aminosilane. Chitosan coated nanoparticles were prepared by three different procedures. Despite well binding efficiency, there were no high residual activities obtained. The highest activity preserved was in case of enzyme, immobilized onto aminosilane coated nanoparticles: 2,06 % at 65,76 % binding efficiency. Immobilized enzyme also demonstrated lower stability at higher pressure and temperature in comparison with free enzyme. Residual activity of free and immobilized enzyme increased by raising temperature at atmospheric conditions.
Keywords:Enzyme immobilization, horseradish peroxidase, maghemite nanoparticles, aminosilane-coated maghemite nanoparticles, chitosan-coated maghemite nanoparticles, binding efficiency, enzyme activity


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