The aim of the proposed diploma thesis is to optimize the procedure of collagen isolation from animal tissues and methods for molecular characterization of isolates. In experimental part, isolations of collagens from animal tissues (chicken, hen, carp, and pork skin) were performed. Total protein concentration was determined by Biuret method and by TNBSA method. Both methods were used also in order to study physiological and thermal stability of the isolates under model conditions. Isolated collagens were characterized at molecular level using PAGE–SDS and microfluidic electrophoresis. Further, amino acids composition and microelement content were analyzed. Finally, the stability of isolated collagens in several types of simulated physiological and pathological conditions was tested too. During isolation relatively sufficient collagen yields were obtained (about 15 % of purified collagen per original mass of biological material). In all analyzed tissues Type I collagen was found. Thermal stability of individual samples differed according to biological source type and tissue age. Viscosimetry measurements confirmed higher stability in collagen samples of older animals. Collagenase exhibited the lowest degradation effect to bovine collagen, while selected mixed microbial hydrolases differed according to enzyme preparative type. Incubation of collagen isolates with selected human pathogens confirmed higher resistance of bovine collagen to biofilm formation when compared with the chicken one.
Identifer | oai:union.ndltd.org:nusl.cz/oai:invenio.nusl.cz:216607 |
Date | January 2010 |
Creators | Mikulíková, Zuzana |
Contributors | Drábková, Michaela, Márová, Ivana |
Publisher | Vysoké učení technické v Brně. Fakulta chemická |
Source Sets | Czech ETDs |
Language | Czech |
Detected Language | English |
Type | info:eu-repo/semantics/masterThesis |
Rights | info:eu-repo/semantics/restrictedAccess |
Page generated in 0.0019 seconds