Please use this identifier to cite or link to this item:
Title: Preparation, characterization and optimization of chitosan nanoparticles as carrier for immobilization of thermophilic recombinant esterase
Authors: İlgü, Hüseyin
Turan, Taylan
Şanlı Mohamed, Gülşah
İlgü, Hüseyin
Turan, Taylan
Şanlı Mohamed, Gülşah
Izmir Institute of Technology. Chemistry
Keywords: Esterase
Issue Date: Sep-2011
Publisher: Taylor and Francis Ltd.
Source: İlgü, H., Turan, T., and Şanlı Mohamed, G. (2011). Preparation, characterization and optimization of chitosan nanoparticles as carrier for immobilization of thermophilic recombinant esterase. Journal of Macromolecular Science, Part A: Pure and Applied Chemistry, 48(9), 713-721. doi:10.1080/10601325.2011.596050
Abstract: Immobilization of biologically important molecules on myriad nano-sized materials has attracted great attention. Through this study, thermophilic esterase enzyme was obtained using recombinant DNA technology and purified applying one-step His-Select HF nickel affinity gel. The synthesis of chitosan was achieved from chitin by deacetylation process and degree of deacetylation was calculated as 89% by elemental analysis. Chitosan nanoparticles were prepared based on the ionic gelation of chitosan with tripolyphosphate anions. The physicochemical properties of the chitosan and chitosan nanoparticles were determined by several methods including SEM (Scanning Electron Microscopy), FT-IR (Fourier Transform Infrared Spectroscopy) and DLS (Dynamic Light Scattering). The morphology of chitosan nanoparticles was spherical and the nanospheres' average diameter was 75.3 nm. The purified recombinant esterase was immobilized efficiently by physical adsorption onto chitosan nanoparticles and effects of various immobilization conditions were investigated in details to develope highly cost-effective esterase as a biocatalyst to be utilized in biotechnological purposes. The optimal conditions of immobilization were determined as follows; 1.0 mg/mL of recombinant esterase was immobilized on 1.5 mg chitosan nanoparticles for 30 min at 60C, pH 7.0 under 100 rpm stirring speed. Under optimized conditions, immobilized recombinant esterase activity yield was 88.5%. The physicochemical characterization of enzyme immobilized chitosan nanoparticles was analyzed by SEM, FT-IR and AFM (Atomic Force Microscopy).
ISSN: 1060-1325
Appears in Collections:Chemistry / Kimya
Scopus İndeksli Yayınlar Koleksiyonu / Scopus Indexed Publications Collection
WoS İndeksli Yayınlar Koleksiyonu / WoS Indexed Publications Collection

Files in This Item:
File Description SizeFormat 
4947.pdfMakale638.63 kBAdobe PDFThumbnail
Show full item record

CORE Recommender


checked on Sep 11, 2021


checked on Sep 11, 2021

Page view(s)

checked on Sep 17, 2021


checked on Sep 17, 2021

Google ScholarTM



Items in GCRIS Repository are protected by copyright, with all rights reserved, unless otherwise indicated.