Scopus İndeksli Yayınlar Koleksiyonu / Scopus Indexed Publications Collection
Permanent URI for this collectionhttps://hdl.handle.net/11147/7148
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Conference Object Citation - WoS: 2Citation - Scopus: 1Determination of Aluminum Oxide Thickness on the Annealed Surface of 8000 Series Aluminum Foil by Fourier Transform Infrared Spectroscopy(Springer, 2017) İnanç Uçar, Özlem; Ekin Meşe, Ayten; Birbaşar, Onur; Dündar, Murat; Özdemir, DurmuşAluminum foil produced with prescribed thermomechanical processing route develop oxide film. Alloy chemistry and annealing practices, particularly its duration and exposed temperature, determine the characteristics of the oxide film. The magnitude and characteristics of the oxide film may impair surface features leading to serious problems in some applications, such as coating, printing and in some severe cases failure in formability. Therefore, it is important for the rolling industry to be able to monitor the oxide formation on the foil products and quantify its thickness. Well known methods to measure an oxide thickness that is in the order of nanometer, require meticulous sample preparation techniques, long duration for measurements and sophisticated equipment. However, in this study, a simple and rapid grazing angle attenuated total reflectance infrared (GA-ATR-FTIR) spectroscopic method combined with chemometrics multivariate calibration has been developed for the oxide thickness determination which is validated with x-ray photoelectron spectroscopy (XPS). 3000 and 8000 series aluminum foil materials which were produced by twin roll casting technique were used in this study. Foil samples were annealed at various different temperatures and annealing times in a laboratory scale furnace. Immediately after collecting GA-ATR-FTIR spectra, the 3000 series alloy samples were sent to a laboratory where XPS reference oxide thickness measurements had been performed. Partial Least Squares (PLS) method was used to develop a multivariate calibration model based on FTIR spectra and XPS reference oxide thickness values in order to predict the aluminum oxide thickness. The correlation coefficient of XPS reference oxide thickness values versus grazing angle ATR-FTIR based PLS predicted values was found as 0.9903 the standard error of cross validation (SECV) was found to be 0.29 nm in range of 4.9–14.0 nm for Al2O3. In addition, the standard error of prediction (SEP) for the validation set was 0.24 nm with the model generated with three principal components (PCs). © The Minerals, Metals & Materials Society 2017.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.