Analysis of the Interactions of a Cationic Surfactant (Lauric Arginate) with an Anionic Biopolymer (Pectin): Isothermal Titration Calorimetry, Light Scattering, and Microelectrophoresis

Langmuir ◽  
2009 ◽  
Vol 25 (1) ◽  
pp. 116-122 ◽  
Author(s):  
D. Asker ◽  
J. Weiss ◽  
D. J. McClements
Keyword(s):  
Light Scattering ◽  
Isothermal Titration Calorimetry ◽  
Cationic Surfactant ◽  
Titration Calorimetry ◽  
Lauric Arginate

scholarly journals Towards Reproducible Enzyme Modeling with Isothermal Titration Calorimetry

2021 ◽  
Author(s):  
Felix Ott ◽  
Kersten S. Rabe ◽  
Christof M Niemeyer ◽  
Gudrun Gygli
Keyword(s):  
Quality Control ◽  
Data Analysis ◽  
Light Scattering ◽  
Dynamic Light Scattering ◽  
Isothermal Titration Calorimetry ◽  
Molecular Mechanisms ◽  
Kinetic Studies ◽  
Titration Calorimetry ◽  
Kinetic And Thermodynamic Parameters ◽  
Enzyme Modeling

<div> <p>An experimental workflow to provide detailed information of the molecular mechanisms of enzymes is described. This workflow will help in the application of enzymes in technical processes by providing crucial parameters needed to plan, model and implement biocatalytic processes more efficiently. These parameters are homogeneity of the enzyme sample (HES), kinetic and thermodynamic parameters of enzyme kinetics and binding of reactants to enzymes. The techniques used to measure these properties are dynamic light scattering (DLS), UV-Vis spectrophotometry and isothermal titration calorimetry (ITC) respectively. The workflow is standardized by the use of SOPs and python-scripted data analysis. </p> <p>We have used the NADPH-dependent alcohol dehydrogenase Gre2p as a challenging enzyme to demonstrate the power of this workflow. Our work highlights the utility for combined binding and kinetic studies for such complex multi-substrate reactions and the importance of sample quality control during experiments.</p> </div>

scholarly journals Towards Reproducible Enzyme Modeling with Isothermal Titration Calorimetry

2021 ◽  
Author(s):  
Felix Ott ◽  
Kersten S. Rabe ◽  
Christof M Niemeyer ◽  
Gudrun Gygli
Keyword(s):  
Quality Control ◽  
Data Analysis ◽  
Light Scattering ◽  
Dynamic Light Scattering ◽  
Isothermal Titration Calorimetry ◽  
Molecular Mechanisms ◽  
Kinetic Studies ◽  
Titration Calorimetry ◽  
Kinetic And Thermodynamic Parameters ◽  
Enzyme Modeling

<div> <p>An experimental workflow to provide detailed information of the molecular mechanisms of enzymes is described. This workflow will help in the application of enzymes in technical processes by providing crucial parameters needed to plan, model and implement biocatalytic processes more efficiently. These parameters are homogeneity of the enzyme sample (HES), kinetic and thermodynamic parameters of enzyme kinetics and binding of reactants to enzymes. The techniques used to measure these properties are dynamic light scattering (DLS), UV-Vis spectrophotometry and isothermal titration calorimetry (ITC) respectively. The workflow is standardized by the use of SOPs and python-scripted data analysis. </p> <p>We have used the NADPH-dependent alcohol dehydrogenase Gre2p as a challenging enzyme to demonstrate the power of this workflow. Our work highlights the utility for combined binding and kinetic studies for such complex multi-substrate reactions and the importance of sample quality control during experiments.</p> </div>

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