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Effect of crosslinking on the denaturation of collagen samples from different animal sources
Ladický, Peter ; Muchová, Johana (referee) ; Sedláček, Petr (advisor)
The diploma thesis deals with the preparation, crosslinking and characterization of collagen films from various animal sources. Collagen from pig, Tilapia, horse, cow and crocodile was used to prepare collagen films. Chemical crosslinking agents EDC/NHS and Lyofix were used to crosslink the prepared films. In the experimental part, differential scanning calorimetry (DSC) method was optimized to determine the denaturation temperature of individual collagen films before and after crosslinking. In addition, the ability of films to swell and degrade has been analyzed. The presence of characteristic groups present in the collagen structure was verified using infrared spectroscopy. The sample morphology was analyzed using Scanning Electron Cryomicroscopy (Cryo-SEM). The results show that EDC/NHS is a better collagen crosslinking agent compared to Lyofix. The best source for the preparation of thermally stable films is piggy collagen, whose denaturation temperature after crosslinking with EDC/NHS was about 69 °C and could represent more than adequate substitution for cow collagen, which is currently most used in the field of tissue engineering and food industry.
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Utilization of thermal analysis in study on protein denaturation
Bošeľová, Miriam ; Pekař, Miloslav (referee) ; Sedláček, Petr (advisor)
This bachelor thesis deals with the use of techniques of thermal analysis in the study of thermal denaturation of proteins. As a model protein was chosen lysozyme. In the experimental part were used two methods of thermal analysis – differential scanning calorimetry (DSC) and temperature modulated differential scanning calorimetry (TMDSC). One of the objectives of the study was to determine the utility of DSC and TMDSC in the study of lysozyme denaturation and to futher characterize the results we can obtain from the individual methods. Another goal was the optimization of TMDSC. During optimalization of TMDSC heat-iso, heat-only and heat-cool modes were compared in 60 seconds and 100 second periods. By selected methods was observed denaturation of lysozyme. Denaturation of lysozyme is predominantly created by reversible component of the heat flow and the denaturation temperature is in the range of 71,16 °C to 75,21 °C depending on the set parameters.
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Effect of crosslinking on the denaturation of collagen samples from different animal sources
Ladický, Peter ; Muchová, Johana (referee) ; Sedláček, Petr (advisor)
The diploma thesis deals with the preparation, crosslinking and characterization of collagen films from various animal sources. Collagen from pig, Tilapia, horse, cow and crocodile was used to prepare collagen films. Chemical crosslinking agents EDC/NHS and Lyofix were used to crosslink the prepared films. In the experimental part, differential scanning calorimetry (DSC) method was optimized to determine the denaturation temperature of individual collagen films before and after crosslinking. In addition, the ability of films to swell and degrade has been analyzed. The presence of characteristic groups present in the collagen structure was verified using infrared spectroscopy. The sample morphology was analyzed using Scanning Electron Cryomicroscopy (Cryo-SEM). The results show that EDC/NHS is a better collagen crosslinking agent compared to Lyofix. The best source for the preparation of thermally stable films is piggy collagen, whose denaturation temperature after crosslinking with EDC/NHS was about 69 °C and could represent more than adequate substitution for cow collagen, which is currently most used in the field of tissue engineering and food industry.
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Utilization of thermal analysis in study on protein denaturation
Bošeľová, Miriam ; Pekař, Miloslav (referee) ; Sedláček, Petr (advisor)
This bachelor thesis deals with the use of techniques of thermal analysis in the study of thermal denaturation of proteins. As a model protein was chosen lysozyme. In the experimental part were used two methods of thermal analysis – differential scanning calorimetry (DSC) and temperature modulated differential scanning calorimetry (TMDSC). One of the objectives of the study was to determine the utility of DSC and TMDSC in the study of lysozyme denaturation and to futher characterize the results we can obtain from the individual methods. Another goal was the optimization of TMDSC. During optimalization of TMDSC heat-iso, heat-only and heat-cool modes were compared in 60 seconds and 100 second periods. By selected methods was observed denaturation of lysozyme. Denaturation of lysozyme is predominantly created by reversible component of the heat flow and the denaturation temperature is in the range of 71,16 °C to 75,21 °C depending on the set parameters.
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