Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

Accelerated biocatalyst stability testing for process optimization.

Phillip R Gibbs1, Christian S Uehara, Urban Neunert

  • 1School of Chemical and Biomolecular Engineering, Parker H. Petit Institute of Bioengineering and Biosciences, Georgia Institute of Technology, 315 Ferst Drive, Atlanta, Georgia 30332-0363, USA.

Biotechnology Progress
|June 4, 2005
PubMed
Summary
This summary is machine-generated.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Metabolic thermodynamics: pertinent reference state and energy potentials.

The FEBS journal·2026
Same author

In situ characterization of amine-forming enzymes shows altered oligomeric state.

Protein science : a publication of the Protein Society·2024
Same author

Improvement of α-amino Ester Hydrolase Stability via Computational Protein Design.

The protein journal·2023
Same author

EnzymeML: seamless data flow and modeling of enzymatic data.

Nature methods·2023
Same author

Mutations Increasing Cofactor Affinity, Improve Stability and Activity of a Baeyer-Villiger Monooxygenase.

ACS catalysis·2022
Same author

Selectivity and kinetic modeling of penicillin G acylase variants for the synthesis of cephalexin under a broad range of substrate concentrations.

Biotechnology and bioengineering·2022

Protein biocatalyst deactivation limits their application. This study presents a new model and accelerated method to determine key kinetic and thermodynamic constants for improved biocatalyst design and stability.

Area of Science:

  • Biocatalysis
  • Enzyme kinetics
  • Protein deactivation

Background:

  • Protein biocatalysts deactivate over time, limiting their practical applications, especially at elevated temperatures.
  • Understanding deactivation mechanisms is crucial for developing more stable and efficient biocatalysts.

Purpose of the Study:

  • To derive a predictive model for biocatalyst activity considering time and temperature.
  • To develop an accelerated method for determining kinetic and thermodynamic parameters of biocatalyst systems.

Main Methods:

  • Utilized transition state theory and the Lumry-Eyring model to formulate a deactivation equation.
  • Derived an analytical solution for total turnover number (ttn) under isothermal conditions.
  • Employed an immobilized glucose isomerase in a CSTR with a linear temperature ramp.

Related Experiment Videos

Main Results:

  • Developed a model predicting biocatalyst behavior as a function of catalytic constant (kcat), unfolding equilibrium constant (K), and deactivation rate constants (k(d,i)).
  • Demonstrated an accelerated method for extracting thermodynamic and kinetic constants using a linear temperature ramp.
  • Experimental results validated the model's predictions for biocatalyst behavior.

Conclusions:

  • The derived model accurately describes time- and temperature-dependent biocatalyst activity.
  • The accelerated method provides an efficient way to characterize biocatalyst systems.
  • Findings contribute to the rational design of more robust and stable protein biocatalysts.