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Immobilization of uricase onto graphene oxide

Immobilization of uricase onto graphene oxide was done by using two different methods, physical adsorption and also chemical modification of the surface of graphene oxide by using N’-(3-(dimethylamino)propyl)carbodiimide (EDC) and N-hydroxysuccinimide (NHS) as cross-linkers. Graphene oxide is proved...

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Main Author: Sidek, Nur Amirah
Format: Project Paper Report
Language:English
Published: 2015
Online Access:http://psasir.upm.edu.my/id/eprint/85055/1/FBSB%202015%20121%20-%20IR.pdf
http://psasir.upm.edu.my/id/eprint/85055/
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spelling my.upm.eprints.850552021-07-13T04:45:12Z http://psasir.upm.edu.my/id/eprint/85055/ Immobilization of uricase onto graphene oxide Sidek, Nur Amirah Immobilization of uricase onto graphene oxide was done by using two different methods, physical adsorption and also chemical modification of the surface of graphene oxide by using N’-(3-(dimethylamino)propyl)carbodiimide (EDC) and N-hydroxysuccinimide (NHS) as cross-linkers. Graphene oxide is proved to be an excellent carrier for uricase immobilization due to it having a large surface area and abundant functional groups. The enzyme immobilization on graphene oxide can be done readily without using any cross-linking reagents or other additional surface modification. It can also be done by modifying the surface of graphene oxide for an enhanced performance. In this study, apart from using different methods, other paramaters such as the concentration of graphene oxide and also enzyme unit used are also varied to determine the best conditions for an optimum performance of the immobilized enzyme. The results obtained indicate that the immobilized enzyme perform better by using the chemical modification method, and the best parameters of uricase immobilization by this method were found as 1 mg/mL graphene oxide concentration and 1 u/ml uricase. 2015-06 Project Paper Report NonPeerReviewed text en http://psasir.upm.edu.my/id/eprint/85055/1/FBSB%202015%20121%20-%20IR.pdf Sidek, Nur Amirah (2015) Immobilization of uricase onto graphene oxide. [Project Paper Report]
institution Universiti Putra Malaysia
building UPM Library
collection Institutional Repository
continent Asia
country Malaysia
content_provider Universiti Putra Malaysia
content_source UPM Institutional Repository
url_provider http://psasir.upm.edu.my/
language English
description Immobilization of uricase onto graphene oxide was done by using two different methods, physical adsorption and also chemical modification of the surface of graphene oxide by using N’-(3-(dimethylamino)propyl)carbodiimide (EDC) and N-hydroxysuccinimide (NHS) as cross-linkers. Graphene oxide is proved to be an excellent carrier for uricase immobilization due to it having a large surface area and abundant functional groups. The enzyme immobilization on graphene oxide can be done readily without using any cross-linking reagents or other additional surface modification. It can also be done by modifying the surface of graphene oxide for an enhanced performance. In this study, apart from using different methods, other paramaters such as the concentration of graphene oxide and also enzyme unit used are also varied to determine the best conditions for an optimum performance of the immobilized enzyme. The results obtained indicate that the immobilized enzyme perform better by using the chemical modification method, and the best parameters of uricase immobilization by this method were found as 1 mg/mL graphene oxide concentration and 1 u/ml uricase.
format Project Paper Report
author Sidek, Nur Amirah
spellingShingle Sidek, Nur Amirah
Immobilization of uricase onto graphene oxide
author_facet Sidek, Nur Amirah
author_sort Sidek, Nur Amirah
title Immobilization of uricase onto graphene oxide
title_short Immobilization of uricase onto graphene oxide
title_full Immobilization of uricase onto graphene oxide
title_fullStr Immobilization of uricase onto graphene oxide
title_full_unstemmed Immobilization of uricase onto graphene oxide
title_sort immobilization of uricase onto graphene oxide
publishDate 2015
url http://psasir.upm.edu.my/id/eprint/85055/1/FBSB%202015%20121%20-%20IR.pdf
http://psasir.upm.edu.my/id/eprint/85055/
_version_ 1706958795025940480
score 13.211869

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