WoS İndeksli Yayınlar Koleksiyonu / WoS Indexed Publications Collection

Permanent URI for this collectionhttps://hdl.handle.net/11147/7150

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Publisher: search.filters.publisher.Elsevier Ltd.Subject: search.filters.subject.Enzyme immobilization

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  • Article
    Citation - WoS: 43
    Citation - Scopus: 42
    Immobilization of Superoxide Dismutase/Catalase Onto Polysulfone Membranes To Suppress Hemodialysis-Induced Oxidative Stress: a Comparison of Two Immobilization Methods
    (Elsevier Ltd., 2015) Yaşar Mahlıçlı, Filiz; Şen, Yasin; Mutlu, Mehmet; Alsoy Altınkaya, Sacide
    The objective of this study is to improve the blood compatibility of polysulfone (PSF) based hemodialysis membranes through generating antioxidative surfaces with superoxide dismutase (SOD)/catalase (CAT) enzyme couple immobilization. Enzymes were attached both covalently and ionically on the plasma treated and polyethyleneimine (PEI) deposited membranes, respectively. The loss of enzymes from PEI modified surface at the end of 4 h was found to be relatively higher during storage in phosphate buffered saline (PBS) at pH 7.4 when compared to the enzymes on the plasma treated surface. The kinetic studies indicated that SOD catalyzed the reaction in the diffusion-limited regime at all substrate concentrations and its inactivation by hydrogen peroxide was prevented in the presence of CAT. SOD/CAT coated PSF membranes were capable of reducing the levels of reactive oxygen species in blood and can significantly prolong activated partial thromboplastin time. In addition, both the adsorption of human plasma proteins and platelet activation on all modified membranes decreased significantly compared to the unmodified PSF membranes. Proposed modification methods did not affect high permeability, high mechanical strength or the non-toxic properties of the PSF membranes.
  • Article
    Citation - WoS: 46
    Citation - Scopus: 52
    Effect of Enzyme Location on Activity and Stability of Trypsin and Urease Immobilized on Porous Membranes by Using Layer-By Self-Assembly of Polyelectrolyte
    (Elsevier Ltd., 2010) Guedidi, Sadika; Yürekli, Yılmaz; Deratani, André; Déjardin, Philippe; Innocent, Christophe; Alsoy Altınkaya, Sacide; Roudesli, Sadok; Yemenicioğlu, Ahmet
    The layer-by-layer (LbL) self-assembly of polyelectrolyte is one of the simplest ways to immobilize enzyme on membrane. In this paper, the immobilization of trypsin (TRY) and urease (URE) on polyacrylonitrile based membranes using the LbL assembly technique was presented. The studied systems consisted in bilayered assemblies with the enzyme layer as the outer layer and trilayered assemblies with the enzyme layer as the inner sandwiched layer. The membrane pore size was chosen so that the smaller enzyme TRY was mainly immobilized within the membrane and confined in the porous membrane structure while URE immobilization mainly took place at the membrane surface. No dramatic difference on reactivity was evidenced between these two enzyme locations. The catalytic activity of immobilized enzymes was found to be lower than the free ones in solution but their stability was dramatically enhanced. The higher activity was observed when the enzyme is deposited as the outer layer of the LbL assembly. On the other hand, the more stable catalytic membranes were obtained when the outer layer consists of a polyelectrolyte covering the enzyme layer. © 2010 Elsevier B.V.