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Related Concept Videos

Factors Affecting Activity Coefficient01:17

Factors Affecting Activity Coefficient

The extended Debye-Hückel equation indicates that the activity coefficient of an ion in an aqueous solution at 25°C depends on three partially interdependent properties: the ionic strength of the solution, the charge of the ion, and the ion size. 
The activity coefficient value for an ion is close to one when the solution has almost zero ionic strength, i.e., when the solution shows close to ideal behavior. As the ionic strength of the solution increases from 0 to 0.1 mol/L, a decrease in the...
Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
Thermodynamics: Activity Coefficient01:24

Thermodynamics: Activity Coefficient

Activity is the measure of the effective concentration of the species in solution. It can be expressed as the product of the molar concentration of the species and its activity coefficient. The activity coefficient is a dimensionless quantity and depends on the total ionic strength of the solution.
The activity coefficient is a measure of the deviation from ideal behavior. When the ionic strength of the solution is minimal, the activity coefficient of an ionic species is close to unity, making...
Phosphorylation01:02

Phosphorylation

The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
The Debye–Hückel Theory of Electrolyte Solutions01:27

The Debye–Hückel Theory of Electrolyte Solutions

The Debye–Hückel theory, established by Peter Debye and Erich Hückel in 1923, is a fundamental concept in physical chemistry. It provides an understanding of the behavior of strong electrolytes in solution, particularly explaining their deviations from ideal behavior.The theory is based on Coulombic interactions (the attraction or repulsion between charged particles) between ions in solution. In an ionic solution, oppositely charged ions tend to attract each other. This means that cations...
Thermodynamics: Chemical Potential and Activity01:10

Thermodynamics: Chemical Potential and Activity

The effective concentration of a species in a solution can be expressed precisely in terms of its activity. Activity considers the effect of electrolytes present in the vicinity of the species of interest and depends on the ionic strength of the solution. The activity of a species is expressed as the product of molar concentration and the activity coefficient of the species.
The thermodynamic equilibrium constant is more accurately defined in terms of activity rather than concentration.

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Related Experiment Video

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Defining Substrate Specificities for Lipase and Phospholipase Candidates
08:59

Defining Substrate Specificities for Lipase and Phospholipase Candidates

Published on: November 23, 2016

Enzyme activity in dialkyl phosphate ionic liquids.

Marie F Thomas1, Luen-Luen Li, Jocelyn M Handley-Pendleton

  • 1Department of Chemistry, Brookhaven National Laboratory, P.O. Box 5000, Upton, NY 11973, USA. mthomas@bnl.gov

Bioresource Technology
|October 18, 2011
PubMed
Summary

Enzyme activity, crucial for biotechnology, was tested in various ionic liquids. Dimethyl phosphate ionic liquids generally supported higher enzyme function compared to diethyl phosphate or acetate variants.

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In Vitro Assay to Measure Phosphatidylethanolamine Methyltransferase Activity
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In Vitro Assay to Measure Phosphatidylethanolamine Methyltransferase Activity
09:33

In Vitro Assay to Measure Phosphatidylethanolamine Methyltransferase Activity

Published on: January 5, 2016

Area of Science:

  • Biocatalysis
  • Enzyme Engineering
  • Green Chemistry

Background:

  • Ionic liquids (ILs) are tunable solvents with potential applications in biocatalysis.
  • Understanding enzyme behavior in ILs is critical for developing sustainable industrial processes.
  • Metagenomic enzymes and enzymes from Volvariella volvacea offer diverse catalytic capabilities.

Purpose of the Study:

  • To investigate the activity of selected enzymes in different ionic liquid environments.
  • To determine the impact of varying ionic liquid structures and concentrations on enzyme performance.
  • To identify optimal ionic liquid conditions for enhanced enzyme stability and function.

Main Methods:

  • Enzyme activity assays were performed using para-nitrobenzene carbohydrate derivatives as substrates.
  • Four metagenomic enzymes and one enzyme from Volvariella volvacea were tested.
  • Enzymes were incubated in four distinct ionic liquids: [mmim][dmp], [emim][dmp], [emim][dep], and [emim][OAc] at varying concentrations.

Main Results:

  • Enzymes exhibited highest activity in dimethyl phosphate-based ionic liquids ([mmim][dmp] and [emim][dmp]).
  • Ionic liquids based on acetate ([emim][OAc]) showed moderate support for enzyme activity.
  • Significant activity loss was observed for [emim][dep] above 10% v/v, while other ILs tolerated up to 20% v/v.

Conclusions:

  • Dimethyl phosphate ionic liquids provide a favorable environment for the studied enzymes.
  • Ionic liquid choice and concentration significantly influence enzyme activity, impacting biocatalytic process design.
  • Further research into IL-enzyme interactions can optimize enzymatic processes in sustainable chemistry.