Please use this identifier to cite or link to this item: https://hdl.handle.net/11147/2091
Title: Partial purification of hen egg white lysozyme by ethanol precipitation method and determination of the thermal stability of its lyophilized form
Other Titles: Yumurta akı lisoziminin etanol çöktürme metodu kullanılarak kısmi olarak saflaştırılması ve liyofilize formunun ısıl stabilitesinin belirlenmesi
Authors: Gemili, Seyhun
Umdu, Emin Selahattin
Yaprak, Nilgün
Üstok, Fatma Işık
Yener, Fatih Yalçın Güneş
Mecitoğlu Güçbilmez, Çiğdem
Altınkaya, Sacide
Yemenicioğlu, Ahmet
Keywords: Ethanol precipitation
Hen egg white
Lysozyme
Partial purification
Thermal stability
Enzymes
Issue Date: 2007
Publisher: Türkiye Klinikleri Journal of Medical Sciences
Source: Gemili, S., Umdu, E. S., Yaprak, N., Üstok, F. I., Yener, F. Y. G., Mecitoğlu Güçbilmez, Ç., Altınkaya, S., and Yemenicioğlu, A. (2007). Partial purification of hen egg white lysozyme by ethanol precipitation method and determination of the thermal stability of its lyophilized form. Turkish Journal of Agriculture and Forestry, 31(2), 125-134.
Abstract: Lysozyme 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.
URI: http://hdl.handle.net/11147/2091
ISSN: 1303-6173
1300-011X
1303-6173
Appears in Collections:Chemical Engineering / Kimya Mühendisliği
Food Engineering / Gıda Mühendisliği
Scopus İndeksli Yayınlar Koleksiyonu / Scopus Indexed Publications Collection
TR Dizin İndeksli Yayınlar / TR Dizin Indexed Publications Collection
WoS İndeksli Yayınlar Koleksiyonu / WoS Indexed Publications Collection

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