Established and novel tools to investigate biocatalyst stability |
| |
| Authors: | Andreas S. Bommarius James M. Broering |
| |
| Affiliation: | a School of Chemical and Biomolecular Engineering, Parker H. Petit Institute of Bioengineering and Bioscience, Georgia Institute of Technology, Atlanta, GAb School of Chemistry and Biochemistry, Parker H. Petit Institute of Bioengineering and Bioscience, Georgia Institute of Technology, Atlanta, GA |
| |
| Abstract: | We report on novel developments regarding the influence of temperature and salt on protein biocatalysts. The influence of temperature on the activation, unfolding, and deactivation of enzymes can now be described quantitatively with simple, analytical models. We demonstrate that enzyme deactivation phenomena can be determined via T-ramping and observation of instantaneous rates. We calculate the total turnover number analytically on the basis of the deactivation mechanism. We also report on the latest efforts to quantify the influence of salts on protein biocatalyst stability. While effects cannot yet be rationalized completely, we nevertheless found novel correlations between protein unfolding and deactivation and ion hydration. |
| |
| Keywords: | Accelerated testing enzyme deactivation Hofmeister effects ion hydration Lumry-Eyring model |
| 本文献已被 InformaWorld 等数据库收录！ |
|
