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Enzyme for Eco-friendly Treatment of Chlorite-Contaminated Water

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Published on : Nov 14, 2017

A universal and easy access to safe drinking water is a worldwide concern, given its potential effect on health. Several technologies have been developed and numerous control methods are being used in various countries to treat municipal water supplies in order to decontaminate them. Chlorite is a notable industrial contaminant that affects the quality of drinking water. When the chlorite ions are present in the soil, these can leach into ground water, leading to environmental hazards. A number of research are focused to devise eco-friendly methods for the treatment of chlorite-contaminated water supplies to communities.

Advances Could Unlock Novel Applications in Bioremediation

Harping on greener approaches to clean water, scientists from across several nations have teamed up to study the potential of a unique bacterial enzyme for an eco-friendly treatment of chlorite-contaminated water. Aided by the novel technology of neutron analysis, the international team led by University of Vienna, Austria, conducted experiments at Oak Ridge National Laboratory, the U.S. Department of Energy, and studied the specific enzymatic activity of chlorite dismutase. They demonstrated that the enzyme can be used to convert chlorite into harmless byproducts, by breaking the ions into chloride and oxygen.

The impact of the results reach wider beyond the application of the techniques to treatment of chlorite-contaminated water, since the enzyme could be used to generate free oxygen in nature. The process could open novel applications in applications in biotechnology and bioremediation, notably by using neutrons to study proteins

Neutron Analysis to Shed Light on Catalysis Mechanism of Protein Enzyme

For long, the working of the enzyme chlorite dismutase was shrouded in complexity. This is constrained largely by the lack of potentially effective and easily available technologies that could help researchers invade the crystal structure of the protein molecule to understand the mechanism of the reactions. Of note, the reaction occurs at optimum rate only at specific temperature, concentration and pH ranges. The scientists isolated chlorite dismutase from the nitrogen?fixing cyanobacterial species and used macromolecular neutron diffractometer technology to study the crystal structure.

The details of the study is published online on October 13, 2017 in the journal ACS Catalysis and is supported by the Austrian Science Fund, FWF, among other governmental initiatives.