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Formulation and Engineering of Biomaterials
Citrate and phosphate influence on green fluorescent protein thermal stability
Article first published online: 23 SEP 2010
DOI: 10.1002/btpr.495
Copyright © 2010 American Institute of Chemical Engineers (AIChE)
Additional Information
How to Cite
de Lencastre Novaes, L. C., Mazzola, P. G., Pessoa, A. and Penna, T. C. V. (2011), Citrate and phosphate influence on green fluorescent protein thermal stability. Biotechnol Progress, 27: 269–272. doi: 10.1002/btpr.495
Publication History
- Issue published online: 10 FEB 2011
- Article first published online: 23 SEP 2010
- Accepted manuscript online: 25 AUG 2010 09:26AM EST
- Manuscript Revised: 10 JUN 2010
- Manuscript Received: 2 MAR 2010
- Abstract
- Article
- References
- Cited By
Keywords:
- green fluorescent protein;
- salt;
- citrate;
- phosphate;
- protein stability;
- thermal stability
Abstract
Protein structure and function can be regulated by no specific interactions, such as ionic interactions in the presence of salts. Green fluorescent protein (GFP) shows remarkable structural stability and high fluorescence; its stability can be directly related to its fluorescence output, among other characteristics. GFP is stable under increasing temperatures, and its thermal denaturation is highly reproducible. The aim of this study was to evaluate the thermal stability of GFP in the presence of different salts at several concentrations and exposed to constant temperatures, in a range of 70–95°C. Thermal stability was expressed in decimal reduction time. It was observed that the D-values obtained were higher in the presence of citrate and phosphate, when compared with that obtained in their absence, indicating that these salts stabilized the protein against thermal denaturation. © 2010 American Institute of Chemical Engineers Biotechnol. Prog., 2011