Chemical Engineering / Kimya Mühendisliği
Permanent URI for this collectionhttps://hdl.handle.net/11147/14
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Article Citation - WoS: 30Citation - Scopus: 33Preparation and Characterization of Polyacrylonitrile Membranes Modified With Polyelectrolyte Deposition for Separating Similar Sized Proteins(Elsevier Ltd., 2012) Yaşar Mahlıçlı, Filiz; Alsoy Altınkaya, Sacide; Yürekli, YılmazOne of the challenges faced by ultrafiltration membranes is to separate proteins with a small difference in their molecular weights. Recently, some researchers tried to overcome this problem by using charged membranes. This study examined the use of layer by layer deposition of polyelectrolytes on the chemically-modified polyacyronitrile membrane to increase the selectivity of the ultrafiltration. The membranes were prepared by wet-phase inversion technique and polyethylenimine (PEI) and alginate (ALG) were chosen as cationic and anionic polyelectrolytes for the modification of the surfaces. Sieving coefficient data were obtained with myoglobin and lysozyme as model proteins. The influences of solution pH, ionic strengths of the protein and polyelectrolyte solution and the number of polyelectrolyte bilayers on both selectivity and throughput were investigated. The highest selectivity and throughput were achieved with the 1-bilayer PEI-ALG coated polyacrylonitrile (PAN) membrane. Increasing the number of coating bilayers or the ionic strength of the protein solution or adding salt into the polyelectrolyte coating solution decreased both the maximum selectivity and throughput of the modified membranes.Article Citation - WoS: 46Citation - Scopus: 52Effect 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, AhmetThe 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.
