TR Dizin İndeksli Yayınlar / TR Dizin Indexed Publications Collection
Permanent URI for this collectionhttps://hdl.handle.net/11147/7149
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Research Project Enzim immobilize edilmiş membranların hazırlanması ve karakterizasyonu: membran performanslarının belirlenmesi(2008) Alsoy Altınkaya, Sacide; Yemenicioğlu, Ahmet; Yürekli, Yılmaz; 03.02. Department of Chemical Engineering; 03.08. Department of Food Engineering; 03. Faculty of Engineering; 01. Izmir Institute of TechnologyBu 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: 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; Alsoy Altınkaya, Sacide; Üstok, Fatma Işık; Yener, Fatih Yalçın Güneş; Yemenicioğlu, Ahmet; Altınkaya, Sacide; Yemenicioğlu, Ahmet; 03.02. Department of Chemical Engineering; 03.08. Department of Food Engineering; 03. Faculty of Engineering; 01. Izmir Institute of TechnologyLysozyme 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.