Chemical Engineering / Kimya Mühendisliği
Permanent URI for this collectionhttps://hdl.handle.net/11147/14
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Research Project Enzim immobilize edilmiş membranların hazırlanması ve karakterizasyonu: membran performanslarının belirlenmesi(2008) Alsoy Altınkaya, Sacide; Yemenicioğlu, Ahmet; Yürekli, YılmazBu çalışmada üreaz enzimi polietilenimin (PEI) ve kitosan (CHI) ile modifiye edilmiş poliakrilonitril (PAN) membranları üzerine immobilize edilmiştir. PEI ve CHI ile modifikasyon PAN membranı üzerine adsorbe olan üreaz miktarını etkilemezken, aktiviteler sırayla 2 ve 1.5 kat artış göstermiştir. Membranların üreye karşı gösterdikleri kinetik performans aşağıdaki şekilde bulunmuştur: PAN+PEI+CHI>PAN+PEI>PAN+CHI>PAN. pH 7 ile 9 aralığında modifiye edilmiş membranlar üzerine immobilize edilen üreaz PAN üzerine immobilize edilene göre daha iyi bir aktivite profili sergilemiştir. PAN+CHI ve PAN membranları üzerine immobilize edilen üreaz 30 ve 37 o C’de optimum aktivite gösterirken, PAN+PEI ve PAN+PEI+CHI üzerine immobilizasyon optimum aktivitenin gözlendiği sıcaklığın 50 ve 60 o C’ye yükselmesine neden olmuştur.Article Citation - WoS: 153Citation - Scopus: 192Development of Cellulose Acetate Based Antimicrobial Food Packaging Materials for Controlled Release of Lysozyme(Elsevier Ltd., 2009) Gemili, Seyhun; Yemenicioğlu, Ahmet; Alsoy Altınkaya, SacideAntimicrobial packaging materials were obtained by incorporation of lysozyme into cellulose acetate (CA) films. In order to achieve controlled release of lysozyme, the structure of the films was changed from highly asymmetric and porous to dense by modulating the composition of the initial casting solution. The highest release rate, soluble lysozyme activity and antimicrobial activity were obtained with the film prepared from 5% CA solution including 1.5% lysozyme. Increasing CA content in the casting solution decreased the porosity of the films, hence, reduced the release rate, maximum released lysozyme activities and the antimicrobial activities of the films. In contrast, immobilized lysozyme activities and the tensile strength of the films increased. The incorporation of lysozyme did not cause significant reductions in tensile strength and elongation at break values except in films prepared with 15% CA. This study showed the good potential of asymmetric CA films to achieve controlled release in antimicrobial packaging.Article Citation - WoS: 87Citation - Scopus: 111Development of Antioxidant Food Packaging Materials With Controlled Release Properties(Elsevier Ltd., 2010) Gemili, Seyhun; Yemenicioğlu, Ahmet; Alsoy Altınkaya, SacideIn this study, cellulose acetate (CA) films with different morphological features were prepared in order to control the release rates of low molecular weight natural antioxidants, L-ascorbic acid and L-tyrosine. Increasing CA content in the casting solution decreased the average pore size and porosity of the films, thus, reduced the diffusion rates of both antioxidants through the films. Although both antioxidants have similar molecular weights, L-tyrosine released into water much more slowly than L-ascorbic acid. The highest antioxidant activity in release test solutions was observed with highly porous L-tyrosine containing films. However, when the porosity of the films reduced, the antioxidant activity of L-ascorbic acid released into solution was found to be higher due to trapping of significant amount of L-tyrosine in dense films. The use of different antioxidants caused different changes in morphological and mechanical properties of the CA films. Varying the structural features of the films with the preparation conditions or using different surfaces of the films allowed the controlled release of each antioxidant. © 2009 Elsevier Ltd. All rights reserved.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.Article Citation - WoS: 11Citation - Scopus: 16Partial Purification of Hen Egg White Lysozyme by Ethanol Precipitation Method and Determination of the Thermal Stability of Its Lyophilized Form(Türkiye Klinikleri Journal of Medical Sciences, 2007) Gemili, Seyhun; Umdu, Emin Selahattin; Yaprak, Nilgün; Üstok, Fatma Işık; Yener, Fatih Yalçın Güneş; Mecitoğlu Güçbilmez, Çiğdem; Altınkaya, Sacide; Yemenicioğlu, AhmetLysozyme was partially purified from hen egg white by precipitation of non-lysozyme protein impurities during incubation in the prence of ethanol. The thermal stability of the obtained partially purified enzyme was also characterized. The incubation of diluted egg white for 2-8 h in the presence of 20% ethanol was not very effective for the partial purification of lysozyme by precipitation of major egg white proteins; however, 4- to 6-h or 6-h to 8-h incubation of diluted egg white in the presence of 30% and 40% ethanol could be employed more effectively for partial purification of lysozyme. Without applying the incubation period, the highest specific activity was obtained by the treatment of egg white with 40% ethanol. Thus, ethanol at this concentration could be used for a continuous process of partial purification. For batch lysozyme purification, on the other hand, incubation in the presence of 30% ethanol was more appropriate. The activities and protein contents of dialyzed and lyophilized enzymes obtained by 6 h-incubation in the presence of 20%, 30%. and 40% ethanol precipitations were 1878, 6669, and 6115 U/mg powder, and 0.98, 0.90, and 0.93 mg protein per mg powder, respectively. The ranges of thermal inactivation parameters, such as D (D80°C = 29.2-59 min, D90°c = 8.8-21 min) and z (Z80-90°c = 17.4-22.3 °C) values of the enzyme, clearly indicated the moderate and variable heat stability of lyophilized lysozymes obtained from different batches of egg white.