Tumturk_2016_Artif.Cells.Nanomed.Biotechnol_44_443

Reference

Title : Acetylcholinesterase immobilized onto PEI-coated silica nanoparticles - Tumturk_2016_Artif.Cells.Nanomed.Biotechnol_44_443
Author(s) : Tumturk H , Yuksekdag H
Ref : Artif Cells Nanomed Biotechnol , 44 :443 , 2016
Abstract :

Polyethyleneimine (PEI) coated-silica nanoparticles were prepared by the Stober method. The formation and the structure of the nanoparticles were characterized by ATR-FT-IR spectroscopy and transmission electron microscopy (TEM). TEM images of the silica and PEI-coated nanoparticles revealed that they were well dispersed and that there was no agglomeration. The acetylcholineesterase enzyme was immobilized onto these nanoparticles. The effects of pH and temperature on the storage stability of the free and immobilized enzyme were investigated. The optimum pHs for free and immobilized enzymes were determined as 7.0 and 8.0, respectively. The optimum temperatures for free and immobilized enzymes were found to be 30.0 and 35.0 degrees C, respectively. The maximum reaction rate (Vmax) and the Michaelis-Menten constant (Km) were investigated for the free and immobilized enzyme. The storage stability of acetylcholinesterase was increased when immobilized onto the novel PEI-coated silica nanoparticles. The reuse numbers of immobilized enzyme were also studied. These hybrid nanoparticles are desirable as carriers for biomedical applications.

PubMedSearch : Tumturk_2016_Artif.Cells.Nanomed.Biotechnol_44_443
PubMedID: 25365355

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Citations formats

Tumturk H, Yuksekdag H (2016)
Acetylcholinesterase immobilized onto PEI-coated silica nanoparticles
Artif Cells Nanomed Biotechnol 44 :443

Tumturk H, Yuksekdag H (2016)
Artif Cells Nanomed Biotechnol 44 :443