Browsing by Author "Cansu, Umran"

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Edible Films Based on Plant and Animal Origin Proteins: Comparison of Some Mechanical and Physicochemical Characteristics
(Wiley, 2025) Okutan, Gulistan; Koc, Gunes; Cansu, Umran; Boran, Gokhan
Edible films were manufactured from three different proteins to evaluate their mechanical strength and some physicochemical features. Wheat gluten (WG), cow hide gelatin (CHG), and cow milk casein (CMC) were used at three different concentrations (5%, 6%, and 7% w/v for WG or 2%, 3%, and 4% w/v for both CHG and CMC) for the film samples. Water activity of the film samples varied within a rather narrow gap, which was between 0.26 and 0.36, with the highest values for WG films and the lowest for CMC. WG and CMC gave basic films while CHG resulted in acidic films with a pH value between 5.6 and 5.7. CHG films showed the highest conductivity while pH and conductivity increased as CHG concentration increased. WG resulted in opaque and dark colored films while CHG and CMC led to almost transparent and light colored films. Water vapor permeability of CMC films was slightly higher compared to CHG and WG counterparts with values around 2.0 x 10-14 g m/s Pa m2. In addition, tensile strength of CHG films was significantly higher than CMC and WG counterparts with values over 25 N/mm2 and more flexible with higher values of Young's modulus and elongation at break. It is concluded that CHG may be utilized by the food industry to manufacture edible films with superior mechanical features along with ease of dissolving and transparent visual characteristics, while WG and CMC might be preferred for more rigid, opaque, and dark colored films as needed.
Kinetic Evaluation of Gelatin Extraction From Chicken Skin and the Effect of Some Extraction Parameters
(Wiley, 2022) Cansu, Umran; Boran, Gokhan
Kinetic models have been extensively studied for the prediction of yield and quality for plant-sourced ingredients although that is very rare for animal-sourced products. This study is designed to evaluate common kinetic models for the prediction of yield in gelatin extraction from chicken skin. Kinetic models used for comparison were the Peleg's, the first order, and the rate law models while extraction parameters studied were solvent pH, solid:liquid ratio, and sample size. Extraction is evaluated based on the protein and hydroxyproline (Hyp) concentrations of each extract. The success of the models is evaluated based on the root-mean-square error (RMSE) and the coefficient of determination (R-2) values calculated for fittings of the models to the experimental data. The protein content of the dried and degreased skin was over 50% before gelatin extraction. Neutral pH led to the highest yield for both protein and Hyp, which were close to 2,100 and 200 mg per 10 g of skin, respectively. Similarly, smaller sample size or lower solid:liquid ratio resulted in a higher yield. In general, the first 60 min of the extraction was by rapid washing and later on by slow diffusion. Peleg's model is found to be the best fit to the experimental data with the highest R-2 values between 0.97 and 0.99 and the lowest RMSE values compared to that of other kinetic models. This is the first report on the kinetics of gelatin extraction as well as one of the few studies on extraction kinetics of animal-sourced products. Practical Applications Extraction parameters including the size of the raw material and raw material:solvent ratio showed significant effects on extraction yield. The smaller the size and the ratio, the higher the yield. Kinetics of gelatin extraction is reported for the first time by this manuscript, dealing with the yield during the whole extraction process. Extraction parameters may create substantial variability in quality and yield; thus, the data presented here may be utilized in minimizing those potential variations, by minimizing the time, energy and solvent required. The gelatin industry may use this report in the design of the gelatin extraction process as the data presented concludes that a high-rate extraction was completed within the first hour of the extraction, leading over 80% of the expected yield. Gelatin manufacturers and researchers in this field may find this manuscript useful as it provides valuable insights on gelatin extraction and its kinetics.
Optimization of a Multi-Step Procedure for Isolation of Chicken Bone Collagen
(Korean Soc Food Science Animal Resources, 2015) Cansu, Umran; Boran, Gokhan
Chicken bone is not adequately utilized despite its high nutritional value and protein content. Although not a common raw material, chicken bone can be used in many different ways besides manufacturing of collagen products. In this study, a multi-step procedure was optimized to isolate chicken bone collagen for higher yield and quality for manufacture of collagen products. The chemical composition of chicken bone was 2.9% nitrogen corresponding to about 15.6% protein, 9.5% fat, 14.7% mineral and 57.5% moisture. The lowest amount of protein loss was aimed along with the separation of the highest amount of visible impurities, non-collagen proteins, minerals and fats. Treatments under optimum conditions removed 57.1% of fats and 87.5% of minerals with respect to their initial concentrations. Meanwhile, 18.6% of protein and 14.9% of hydroxyproline were lost, suggesting that a selective separation of non-collagen components and isolation of collagen were achieved. A significant part of impurities were selectively removed and over 80% of the original collagen was preserved during the treatments.
Physiochemical and Functional Properties of Gelatin Obtained From Tuna, Frog and Chicken Skins
(Elsevier Sci Ltd, 2019) Tumerkan, Elif Tugce Aksun; Cansu, Umran; Boran, Gokhan; Mac Regenstein, Joe; Ozogul, Fatih
Growing demand for gelatin has increased interest in using alternative raw materials. In this study, different animal skins; namely frog, tuna and chicken skins; were utilized in gelatin extraction by previously optimized extraction procedures. Quality characteristics and functional properties of the resultant gelatins were comparatively investigated. Frog skin gelatin had the highest protein content with 77.8% while the highest hydroxyproline content was found in chicken skin gelatin with 6.4%. Frog skin gelatin showed a significantly higher melting point (42.7 degrees C) compared to tuna and chicken gelatins. Bloom value was also significantly higher in frog skin gelatin compared to that of chicken and tuna skin gelatins. Results showed that processing waste like skins of different animals may present opportunities in gelatin production as high quality alternatives. This study may help the industry by providing one hand comparable data over potentially significant sources.