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Accelerated Biocatalyst Stability Testing for Process Optimization
Author(s) -
Gibbs Phillip R.,
Uehara Christian S.,
Neunert Urban,
Bommarius Andreas S.
Publication year - 2008
Publication title -
biotechnology progress
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 129
eISSN - 1520-6033
pISSN - 8756-7938
DOI - 10.1021/bp049609k
Subject(s) - biocatalysis , stability (learning theory) , process (computing) , biochemical engineering , chemistry , computer science , catalysis , engineering , biochemistry , machine learning , ionic liquid , operating system
The deactivation of protein biocatalysts even at relatively low temperatures is one of the principal drawbacks to their use. To aid in the development of novel biocatalysts, we have derived an equation for both time‐ and temperature‐dependent activity of the biocatalyst based on known concepts such as transition state theory and the Lumry‐Eyring model. We then derived an analytical solution for the total turnover number ( ttn ), under isothermal operation, as a function of the catalytic constant k cat , the unfolding equilibrium constant K , and the intrinsic first‐order deactivation rate constant(s) k d,i . Employing an immobilized glucose isomerase biocatalyst in a CSTR and utilizing a linear temperature ramp beyond the T m of the enzyme, we demonstrate an accelerated method for extracting the thermodynamic and kinetic constants describing the biocatalyst system. In addition, we demonstrate that the predicted biocatalyst behavior at different temperatures and reaction times is consistent with the experimental observations.