Master Degree / Yüksek Lisans Tezleri

Permanent URI for this collectionhttps://hdl.handle.net/11147/3008

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  • Master Thesis
    Determination of Cadmium Bound To Whey Proteins by Laser-Induced Breakdown Spectroscopy at Low Pressures
    (2023) Yalçın, Şerife; Yaman, İlayda; Yalçın, Şerife Hanım; 04.01. Department of Chemistry; 04. Faculty of Science; 01. Izmir Institute of Technology
    In this thesis study, a dried-droplet LIBS methodology at reduced pressures for determining cadmium in aqueous media and in biological samples has been developed. With the advantage of the signal enhancement effect at reduced pressures, the optimum pressure for Cd detection was determined. Results were justified with the plasma images taken at different pressures. 100 mbar pressure was found as the optimum for most emission lines of Cd. To find the most suitable substrate onto which analyte droplets will be loaded, silicon wafer-based substrates of different coating types and coating thicknesses were studied. Among them, the c-Si substrate was found to show the highest signal enhancement for Cd detection. The performance of the methodology for quantitative analysis of Cd was shown by standard solutions and certified reference water samples. Calibration curves were constructed, and performance characteristics (limit of detection, accuracy, precision) were evaluated. Detection limits in absolute amounts of 6.8 pg and 1.05 pg were obtained at atmospheric and 100 mbar pressures, respectively. The application studies involve the determination of Cd bound to whey proteins. For this purpose, standard protein (BSA) and whey protein extracted from the milk were incubated in standard Cd solutions for several hours and filtered through cut-off filters via centrifugation. The unreacted cadmium in the filtrate and Cd-bound protein in fraction were analyzed separately. It has been shown that dried-droplet LIBS at reduced pressures is a suitable methodology for identifying and determining Cd and Cd bound to proteins with a picogram amount of detection capability.
  • Master Thesis
    Preparation of Albumin Nanoparticles Using an Ionic Liquid Based Microemulsion-Like Method
    (Izmir Institute of Technology, 2018) Demirkurt, Begüm; Adem, Umut; Akdoğan, Yaşar; Akdoğan, Yaşar; Adem, Umut; 03.09. Department of Materials Science and Engineering; 03. Faculty of Engineering; 01. Izmir Institute of Technology
    Rich drug transportation ability of serum albumin protein has inspired scientists to obtain drug nanocarriers from albumin. In the literature, different methods have been developed to prepare albumin nanoparticles and their drug delivery properties have been studied. Here, this study aims to obtain albumin nanoparticles for a first time using ionic liquid (IL) included systems. Goal of this project is using imidazolium based ionic liquids (green solvent) to prepare albumin nanoparticles as alternative solvents for the commonly used organic solvents. The use of volatile, toxic and flammable organic solvents in the albumin nanoparticle production has various negative effects on both human health and environment. Ionic liquids as non-flammable, non-volatile and non-toxic solvent candidates have attracted considerable attention in recent years both in the literature and in industry. Their ability to solve different types of solutes, designability, special mixing ability with water in IL/water binary systems and environmentally friendly properties cause ILs to overtake traditional organic solvents. This thesis study proposed a novel and environmentally friendly microemulsionlike method for producing albumin nanoparticles in IL/water binary systems. Various experimental parameters such as pH effects, albumin concentrations, water amount, surfactant effects, glutaraldehyde effects, homogenizer effects, etc. were investigated to obtain uniform albumin nanoparticles. As a result, we achieved to synthesize uniformly distributed 200 nm average size albumin nanoparticles at pH 9.0 using 1.5% (w/w) of bovine serum albumin (BSA) in 1-butyl-3-methylimidazolium tetrafluoroborate using TX-100/n-butanol surfactant mixture.
  • Master Thesis
    An Investigation of Morphology of Polymeric Micellar Structures in the Presence of Protein for Drung Delivery Purposes
    (Izmir Institute of Technology, 2016) Kutluay, Gülistan; Polat, Hürriyet; Polat, Hürriyet; 04.01. Department of Chemistry; 04. Faculty of Science; 01. Izmir Institute of Technology
    Polymeric micellar structures are becoming increasingly important in drug delivery applications. Morphology of these structures is a factor determining the form and the amount of the drug to be enveloped as well as how the release mechanisms will function. Though there are numerous work on micelles in the literature in aqueous media, understanding is lacking with respect to the specifics of the micelle formation and the exact morphology of the micelles produced within simulated body fluids (SBF) that also contains protein. In this work, the well-defined micellar structures with and without bovine serum albumin (BSA) in SBF using some selected polymeric surface active agents (PEO-PPO-PEO tri-block copolymer, P-123) were studied. The forms of P-123 molecules in distilled water (DW) and SBF (studied by surface tension measurements), micelle size distributions (studied by AFM, DLS, STEM, TEM), and electro kinetic potentials (studied by DLS) were the main parameters studied. DLS results showed that the average size of P-123 micelles did not change much in the presence of BSA in DW or SBF. In the cases of AFM, STEM and TEM, the sizes of P-123 micelles in the absence of BSA were comparable to the results of DLS. In the presence of BSA, on the other hand, the micelle structures come together to form large and loose aggregates in both DW and SBF. When P-123 micelles loaded with drug, DLS results showed that the presence of drug in micelles does not change the size of micelles much in both water and SBF. But STEM results show a considerable increase in the sizes of P-123 micelles. The drug loaded micelles seem to aggregate in water and SBF in the absence of BSA and in water in the presence of BSA. But they seem to disperse in SBF in the presence of BSA.