Immobilization of Thermophilic Esterase on Magnetic Cornstarch Nanoparticles for Biological Applications

dc.contributor.advisor Şanlı Mohamed, Gülşah
dc.contributor.author Öz, Yasin
dc.date.accessioned 2017-01-31T07:44:28Z
dc.date.available 2017-01-31T07:44:28Z
dc.date.issued 2016
dc.description Thesis (Master)--İzmir Institute of Technology, Chemistry, İzmir, 2016 en_US
dc.description Full text release delayed at author's request until 2016.12.27 en_US
dc.description Includes bibliographical references (leaves: 51-54) en_US
dc.description Text in English; Abstract: Turkish and English en_US
dc.description x, 56 leaves en_US
dc.description.abstract In last three decades, even the role of enzymes for biological and industrial applications has become more worthy, enzymes also have some defects. The enzyme immobilization allows to overcome these defects by improving abilities of reusing of catalysts by multiple times, easier reactor operation and product separation. Due to its potential use in biological and industrial applications, isolated thermophilic esterase from Geobacillus sp. was immobilized on magnetic cornstarch nanoparticles. In order to determine activity performance of immobilized enzyme, the effects of temperature, pH and some chemicals on enzyme activity were investigated. The results have shown that after immobilization, the relative activity of immobilized esterase has increased to 80% at 80 0C in comparison to free esterase. Therewithal, the reusability of immobilized esterase has increased fourfold in comparison to free esterase. The magnetic character of the support media has brought ease to separate biocatalysts from reaction media. en_US
dc.description.abstract Geçtiğimiz son otuz yılda, enzimlerin biyolojik ve endüstriyel uygulamalardaki rolü her ne kadar değerlendiysede, bazı kusurları da vardır. Enzim sabitlemesi, bu kusurların üstesinden gelinerek, katalizörün birçok defa kullanılmasına, reaksion sırasında daha kolay aktivleşmesine ve enzimlerin reaksiyon ortamından kolay ayrılmasına olanak sağlamaktadır. Biyolojik ve endüstriyel uygulamalarda olası kullanımından dolayı, Geobacillus sp. türünden izole edilen termofilik estaraz manyetik mısır nişastası nanoparçacıkları üzerine sabitlendi. Sabitlenmiş enzimin aktivite performansına karar vermek için, sıcaklık, pH ve bazı kimyasal maddelerin bağlı enzim aktivitesi üzerindeki etkileri araştırıldı. Enzimlerin bağlanmasının ardından sonuçlar gösterdi ki, sabitlenmiş esterazın bağıl aktivitesi, serbest enzime kıyasla 80 0C sıcaklıkta %80 arttı. Ayrıca serbest esteraz ile kıyaslandığında, sabitlenmiş esterazın tekrar kullanılabilirliği dört kat arttı. Bağlanılan maddenin manyetik özelliği biyokatalizörleri ortamdan ayırmak için kolaylık sağladı. en_US
dc.identifier.citation Öz, Y. (2016). Immobilization of thermophilic esterase on magnetic cornstarch nanoparticles for biological applications. Unpublished master's thesis, İzmir Institute of Technology, İzmir, Turkey en_US
dc.identifier.uri http://hdl.handle.net/11147/4766
dc.language.iso en en_US
dc.publisher Izmir Institute of Technology en_US
dc.rights info:eu-repo/semantics/openAccess en_US
dc.subject Enzymes en_US
dc.subject Magnetic cornstarch nanoparticles en_US
dc.subject Geobacillus sp. en_US
dc.subject Nanoparticles en_US
dc.title Immobilization of Thermophilic Esterase on Magnetic Cornstarch Nanoparticles for Biological Applications en_US
dc.title.alternative Termofilik Esterazin Biyolojik Çalışmalar için Manyetik Mısır Nişastası Nanoparçacıkları Üzerine Bağlanması en_US
dc.type Master Thesis en_US
dspace.entity.type Publication
gdc.author.institutional Öz, Yasin
gdc.coar.access open access
gdc.coar.type text::thesis::master thesis
gdc.description.department Thesis (Master)--İzmir Institute of Technology, Chemistry en_US
gdc.description.publicationcategory Tez en_US
gdc.description.scopusquality N/A
gdc.description.wosquality N/A
relation.isAuthorOfPublication.latestForDiscovery eae23f7d-4b68-4072-9e21-c5a4a8c41aa3
relation.isOrgUnitOfPublication.latestForDiscovery 9af2b05f-28ac-4011-8abe-a4dfe192da5e

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