Immobilization and characterization of recombinant esterase enzyme on chitosan nanoparticles

Ilgü, Hüseyin; Turan, Taylan; Şanli-Mohameda, Gülşa (2011). Immobilization and characterization of recombinant esterase enzyme on chitosan nanoparticles. Journal of macromolecular science. Part A - pure and applied chemistry, 48(9), pp. 713-721. Taylor & Francis 10.1080/10601325.2011.596050

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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 60°C, 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).

Item Type:

Journal Article (Original Article)

Division/Institute:

04 Faculty of Medicine > Pre-clinic Human Medicine > Institute of Biochemistry and Molecular Medicine

UniBE Contributor:

Ilgü, Hüseyin

Subjects:

500 Science > 570 Life sciences; biology
600 Technology > 610 Medicine & health

ISSN:

1060-1325

Publisher:

Taylor & Francis

Language:

German

Submitter:

Factscience Import

Date Deposited:

04 Oct 2013 14:23

Last Modified:

07 Apr 2014 18:31

Publisher DOI:

10.1080/10601325.2011.596050

Web of Science ID:

000299745500006

URI:

https://boris.unibe.ch/id/eprint/8149 (FactScience: 213637)

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