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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.
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Bommarius et al. (2005) studied this question.
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