<abstract xmlns="http://www.w3.org/1999/xhtml">The analysis of UV-VIS spectrum was used for testing changes through 36 days and the impact of external conditions (reduced temperature (R), microwave radiation (M) and normal conditions (NC) for comparisons) on the stability of: BSA and BSA-Fe2+ complexes after different treating procedure. The increase of BSA absorption with increasing concentration of Fe2+ was observed. Increased absorption of BSA, and BSA-Fe2+ with time, related probably to conformational changes present in the protein and changes in electrostatic reactions within the BSA-Fe2+ complexes. Examination of the impact of an external factor on stabilization of the protein and complexes showed a tendency to keep the stability under reduced temperature and a trend with accelerated protein and complex aging under microwave radiation. The observed tendencies to changes under the influence of external factors became more significant in time. These effects were most probably related to changes of the protein structure and time, while the observed trend of accelerating the changes was impacted by the applied external factors.</abstract>

The analysis of UV-VIS spectrum was used for testing changes through 36 days and the impact of external conditions (reduced temperature (R), microwave radiation (M) and normal conditions (NC) for comparisons) on the stability of: BSA and BSA-Fe2+ complexes after different treating procedure. The increase of BSA absorption with increasing concentration of Fe2+ was observed. Increased absorption of BSA, and BSA-Fe2+ with time, related probably to conformational changes present in the protein and changes in electrostatic reactions within the BSA-Fe2+ complexes. Examination of the impact of an external factor on stabilization of the protein and complexes showed a tendency to keep the stability under reduced temperature and a trend with accelerated protein and complex aging under microwave radiation. The observed tendencies to changes under the influence of external factors became more significant in time. These effects were most probably related to changes of the protein structure and time, while the observed trend of accelerating the changes was impacted by the applied external factors.

Investigation of Biosensor Potential Component Stability Caused by Influence of External Condition

Department of Computer Science and Automatics, Faculty of Mechanical Engineering and Computer Science

Ecological Chemistry and Engineering S

This work is licensed under the Creative Commons Attribution-NonCommercial-NoDerivatives 3.0 License.

The analysis of UV-VIS spectrum was used for testing changes through 36 days and the impact of external conditions (reduced temperature (R), microwave...

Investigation of Biosensor Potential Component Stability Caused by Influence of External Condition

Publicado en línea: 21 ene 2020

Páginas: 665 - 674

DOI: https://doi.org/10.1515/eces-2019-0048

Palabras clave
biosensor, BSA, UV-Vis

© 2019 Aleksandra Kłos-Witkowska et al., published by Sciendo

This work is licensed under the Creative Commons Attribution-NonCommercial-NoDerivatives 3.0 License.

Investigation of Biosensor Potential Component Stability Caused by Influence of External Condition

Publicado en línea: 21 ene 2020

Páginas: 665 - 674

DOI: https://doi.org/10.1515/eces-2019-0048

Palabras clavebiosensor, BSA, UV-Vis

© 2019 Aleksandra Kłos-Witkowska et al., published by Sciendo

This work is licensed under the Creative Commons Attribution-NonCommercial-NoDerivatives 3.0 License.

Palabras clave
biosensor, BSA, UV-Vis