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Lactic acid, an important organic acid extensively applied in food, pharmaceutical, and biodegradable polymer industries, is primarily produced via microbial fermentation. This method is favored over chemical synthesis due to its environmental sustainability and capacity for enantiomerically pure product formation. Among various microbial processes, the fermentation of starch-based substrates stands out due to the abundance and renewability of raw materials like corn and potatoes.Hydrolysis of...

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Updated: Jun 10, 2026

An Assay for Measuring the Activity of Escherichia coli Inducible Lysine Decarboxyase
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Published on: December 19, 2010

Urease activity and L-ascorbic acid.

Barbara Krajewska1, Małgorzata Brindell

  • 1Jagiellonian University, Faculty of Chemistry, Kraków, Poland. krajewsk@chemia.uj.edu.pl

Journal of Enzyme Inhibition and Medicinal Chemistry
|August 11, 2010
PubMed
Summary

Ascorbic acid (AA) inactivates urease by lowering pH in unbuffered solutions. In buffered systems, AA and dehydroascorbic acid (DHA) inhibit urease primarily via hydrogen peroxide, especially with Fe(3+).

Area of Science:

  • Biochemistry
  • Enzymology
  • Antimicrobial Research

Background:

  • Urease is a key enzyme in various biological processes.
  • L-ascorbic acid (AA) and its oxidized form, dehydroascorbic acid (DHA), are important biological antioxidants.
  • Understanding urease inhibition is crucial for treating ureolytic bacterial infections, such as those caused by Helicobacter pylori.

Purpose of the Study:

  • To investigate the behavior of urease in the presence of AA and DHA under different conditions.
  • To elucidate the mechanisms of urease inactivation by AA and DHA.
  • To explore the potential role of AA in therapies targeting ureolytic bacteria.

Main Methods:

  • Enzyme inactivation studies of urease were performed in both unbuffered and buffered systems.

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  • The influence of AA, DHA, Fe(3+) ions, and pH on urease activity was assessed.
  • Mechanisms of inhibition, including pH-dependent denaturation and thiol oxidation, were investigated.

    • Main Results:

    • In unbuffered systems, AA inactivated urease biphasically due to pH-lowering denaturation.
    • In buffered systems, AA and DHA alone did not inhibit urease.
    • Inhibition by AA and DHA was observed in the presence of Fe(3+) ions, primarily mediated by hydrogen peroxide (H(2)O(2)).
    • DHA-Fe(3+) inhibition involved enzyme thiol oxidation and was more effective at higher pH.

    Conclusions:

    • The mechanism of urease inhibition by AA and DHA is condition-dependent.
    • Hydrogen peroxide plays a critical role in the inhibitory action of AA and DHA in the presence of Fe(3+).
    • These findings offer insights into the potential therapeutic applications of AA in combating ureolytic bacterial infections.