Chemical Engineering / Kimya Mühendisliği
Permanent URI for this collectionhttps://hdl.handle.net/11147/14
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Article Kinetic and Structural Characterization of Interaction Between Trypsin and Equisetum Arvense Extract(Türk Biyokimya Derneği, 2014) Uslu, Mehmet Emin; Bayraktar, Oğuz; Ceylan, ÇağatayObjective: In this study the inhibitory effect of E. arvense extract on trypsin activity and the effect of trypsin on E. arvense extract were studied. In addition the nature of the interaction between the extract and trypsin was investigated. Methods: The inhibitory effect ethanol extract of E. arvense on trypsin activity was determined using trypsin enzyme assay. The structural effects of the extract-trypsin interaction for the extract were analyzed by FTIR. Finally, the HPLC analyses were carried out to analyze the individual components of the extract and the supernatant and soluble precipitate phases. Results: E. arvense extract was found to decrease total percent activity of trypsin to 5% in 24 hour at 24 °C. FTIR analyses indicated that the interaction between trypsin and E. arvense extract caused changes in the structure and hydrogen bonding behavior and composition of the extract proteins. These interactions also caused the extract lipids to accumulate in the insoluble precipitate phase. Most of the phenolics remained in the supernatant phase enhancing the inactivation of trypsin. However, the precipitated compounds were shown to be of apolar in nature as shown in the HPLC chromatograms. Conclusion: The methods that were used showed that the high phenolic content of E. arvense was the main reason for the inhibition of trypsin enzyme activity by denaturing the enzyme.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.