Person:
KAHRAMAN, MEMET VEZİR

Profile Picture

Email Address

Birth Date

Research Projects

Organizational Units

OrgUnit Logo
Organizational Unit

Job Title

Last Name

KAHRAMAN

First Name

MEMET VEZİR

Name

Filters

2006 - 200912010 - 20181
Reset filters

Settings

Author: OGAN, AYŞE × Subject: STABILITY ×

Search Results

Now showing 1 - 2 of 2
  • No Thumbnail Available
    PublicationMetadata only
    Soybean oil based resin: A new tool for improved immobilization of alpha-amylase
    (WILEY, 2006) OGAN, AYŞE; Kahraman, MV; Kayaman-Apohan, N; Ogan, A; Gungor, A
    Acrylated epoxidized soybean resin has been utilized to immobilize the alpha-amylase via UV-curing technique. Among the numerous methods that exist for enzyme immobilization, entrapment and covalent binding are the focus of this study. The properties of immobilized enzyme were investigated and compared with those of the free enzyme. Upon immobilization by the two methods, the catalytic properties of the enzyme were not considerably changed as compared with that of nonimmobilized form; enzyme. The free enzyme lost its activity completely in 20 days, where as storage and repeated usage capability experiments demonstrated higher stability for the immobilized form. Immobilized enzyme prepared by attachment method possesses relatively higher activity compared with the activity of those obtained by entrapment method. (c) 2006 Wiley Periodicals, Inc.
  • Thumbnail Image
    PublicationOpen Access
    Covalent immobilization of acetylcholinesterase on a novel polyacrylic acid-based nanofiber membrane
    (WILEY, 2018-04) OGAN, AYŞE; Cakiroglu, Bekir; Cigil, Asli Beyler; Ogan, Ayse; Kahraman, M. Vezir; Demir, Serap
    In this study, polyacrylic acid-based nanofiber (NF) membrane was prepared via electrospinning method. Acetylcholinesterase (AChE) from Electrophorus electricus was covalently immobilized onto polyacrylic acid-based NF membrane by demonstrating efficient enzyme immobilization, and immobilization capacity of polymer membranes was found to be 0.4 mg/g. The novel NF membrane was synthesized via thermally activated surface reconstruction, and activation with carbonyldiimidazole upon electrospinning. The morphology of the polyacrylic acid-based membrane was investigated by scanning electron microscopy, Fourier Transform Infrared Spectroscopy, and thermogravimetric analysis. The effect of temperature and pH on enzyme activity was investigated and maxima activities for free and immobilized enzyme were observed at 30 and 35 degrees C, and pH 7.4 and 8.0, respectively. The effect of 1 mM Mn2+, Ni2+, Cu2+, Zn2+, Mg2+, Ca2+ ions on the stability of the immobilized AChE was also investigated. According to the Michaelis-Menten plot, AChE possessed a lower affinity to acetylthiocholine iodide after immobilization, and the Michaelis-Menten constant of immobilized and free AChE were found to be 0.5008 and 0.4733 mM, respectively. The immobilized AChE demonstrated satisfactory reusability, and even after 10 consecutive activity assay runs, AChE maintained ca. 87% of its initial activity. Free enzyme lost its activity completely within 60 days, while the immobilized enzyme retained approximately 70% of the initial activity under the same storage time. The favorable reusability of immobilized AChE enables the support to be employable to develop the AChE-based biosensors.