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Title:Stabilnost inkapsulirane hrenove peroksidaze : diplomsko delo univerzitetnega študijskega programa I. stopnje
Authors:ID Macur, Mitja (Author)
ID Leitgeb, Maja (Mentor) More about this mentor... New window
ID Vasić, Katja (Comentor)
Files:.pdf UN_Macur_Mitja_2020.pdf (2,55 MB)
MD5: FF2E97C65EBBB34A3935E2483690AC7E
PID: 20.500.12556/dkum/a9237384-0939-49df-8c0a-467b9e7edb93
 
Language:Slovenian
Work type:Bachelor thesis/paper
Typology:2.11 - Undergraduate Thesis
Organization:FKKT - Faculty of Chemistry and Chemical Engineering
Abstract:Namen diplomskega dela je obsegal pripravo imobilizirane hrenove peroksidaze (HRP), in sicer inkapsulirane v obliki alginatnih kroglic, določanje preostale aktivnosti inkapsulirane HRP ter določanje aktivnosti inkapsulirane HRP po skladiščenju pri temperaturah -18 °C, 4 °C, 22 °C in 30 °C. Encim HRP smo inkapsulirali v natrijev alginatni hidrogel z metodo ionotropnega geliranja v raztopini kalcijevega klorida (CaCl2) v obliki sferičnih kroglic. Vzorce kroglic z inkapsulirano HRP smo razdelili na 2 dela ter jih skladiščili v natrijevem acetatnem pufru (pH = 7,8) in na suhem v petrijevki. Rezultate smo primerjali s preostalo aktivnostjo HRP v raztopini in ovrednotili vpliv in način skladiščenja na aktivnost inkapsulirane HRP z izbranim nosilcem. Ugotovili smo nezanemarljiv vpliv alginatnega nosilca na preostalo aktivnost HRP. Rezultati kažejo, da alginatni nosilec učinkovito izboljša aktivnost HRP, medtem ko podaljšanja uporabnosti nismo potrdili. Inkapsulirani HRP v pufru se preostala aktivnost pri temperaturah skladiščenja -18 °C in 4 °C s časom povečuje in je v začetku nižja od preostale aktivnosti HRP, skladiščene pri višji temperaturi. Kot najbolj primeren način se izkaže skladiščenje inkapsulirane HRP v pufru, četudi smo potrdili njeno uhajanje iz alginatnih kroglic.
Keywords:imobilizacija, hrenova peroksidaza, inkapsulacija, natrijev alginat, encimska aktivnost
Place of publishing:Maribor
Place of performance:Maribor
Publisher:[M. Macur]
Year of publishing:2020
Number of pages:61 f.
PID:20.500.12556/DKUM-78054 New window
UDC:66.02(043.2)
COBISS.SI-ID:36418307 New window
NUK URN:URN:SI:UM:DK:RLQNETKW
Publication date in DKUM:09.11.2020
Views:1286
Downloads:121
Metadata:XML DC-XML DC-RDF
Categories:KTFMB - FKKT
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Licences

License:CC BY-NC-ND 4.0, Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International
Link:http://creativecommons.org/licenses/by-nc-nd/4.0/
Description:The most restrictive Creative Commons license. This only allows people to download and share the work for no commercial gain and for no other purposes.
Licensing start date:12.10.2020

Secondary language

Language:English
Title:Stability of encapsulated horseradish peroxidase
Abstract:Our work comprises the preparation of the immobilized horseradish peroxidase (HRP), encapsulated in the form of alginate beads, determination of residual activity of encapsulated HRP, and determination of activity of encapsulated HRP following its storage at temperatures of -18 °C, 4 °C, 22 °C, and 30 °C. The HRP enzyme was encapsulated in a sodium alginate hydrogel using ionotropic gelation in a calcium chloride solution (CaCl2) in the form of spherical beads. The samples of beads with encapsulated HRP were divided to two parts, and then stored in a sodium acetate buffer (pH = 7,8) or in a dry place in a petri dish. The results were compared to the residual activity of HRP in the solution, after which we evaluated the impact and method of storage on the activity of the encapsulated HRP with the selected carrier. We determined a significant impact of the alginate carrier on the residual activity of HRP. The results show that the alginate carrier efficiently improves the HRP activity, but no extension of usability was confirmed. The residual activity of the encapsulated HRP in buffer at storage temperatures of -18 °C and 4 °C increases over time, and is initially lower than the residual activity of HRP, stored at a higher temperature. Storage of encapsulated HRP in buffer seems to be the most appropriate method, even though we have confirmed enzyme leakage.
Keywords:immobilization, horseradish peroxidase, sodium alginate, enzyme activity


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