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dc.contributor.authorGemili, Seyhun
dc.contributor.authorUmdu, Emin Selahattin
dc.contributor.authorYaprak, Nilgün
dc.contributor.authorÜstok, Fatma Işık
dc.contributor.authorYener, Fatih Yalçın Güneş
dc.contributor.authorMecitoğlu Güçbilmez, Çiğdem
dc.contributor.authorAltınkaya, Sacide
dc.contributor.authorYemenicioğlu, Ahmet
dc.date.accessioned2016-08-12T07:09:35Z
dc.date.available2016-08-12T07:09:35Z
dc.date.issued2007
dc.identifier.citationGemili, 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.en_US
dc.identifier.issn1303-6173
dc.identifier.urihttp://hdl.handle.net/11147/2091
dc.description.abstractLysozyme 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.en_US
dc.language.isoengen_US
dc.publisherTÜBİTAKen_US
dc.rightsinfo:eu-repo/semantics/openAccessen_US
dc.subjectEthanol precipitationen_US
dc.subjectHen egg whiteen_US
dc.subjectLysozymeen_US
dc.subjectPartial purificationen_US
dc.subjectThermal stabilityen_US
dc.subjectEnzymesen_US
dc.titlePartial purification of hen egg white lysozyme by ethanol precipitation method and determination of the thermal stability of its lyophilized formen_US
dc.title.alternativeYumurta akı lisoziminin etanol çöktürme metodu kullanılarak kısmi olarak saflaştırılması ve liyofilize formunun ısıl stabilitesinin belirlenmesien_US
dc.typearticleen_US
dc.contributor.authorIDTR2091en_US
dc.contributor.authorIDTR2675en_US
dc.contributor.iztechauthorGemili, Seyhun
dc.contributor.iztechauthorUmdu, Emin Selahattin
dc.contributor.iztechauthorYaprak, Nilgün
dc.contributor.iztechauthorÜstok, Fatma Işık
dc.contributor.iztechauthorYener, Fatih Yalçın Güneş
dc.contributor.iztechauthorAltınkaya, Sacide
dc.contributor.iztechauthorYemenicioğlu, Ahmet
dc.relation.journalTurkish Journal of Agriculture and Forestryen_US
dc.contributor.departmentIzmir Institute of Technology. Food Engineeringen_US
dc.contributor.departmentIzmir Institute of Technology. Chemical Engineering
dc.identifier.volume31en_US
dc.identifier.issue2en_US
dc.identifier.startpage125en_US
dc.identifier.endpage134en_US
dc.identifier.wosWOS:000247897800006
dc.identifier.scopusSCOPUS:2-s2.0-34447547715
dc.relation.publicationcategoryMakale - Ulusal Hakemli Dergi - Kurum Öğretim Elemanıen_US


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