Atrazine (2-chloro-4-ethylamino-6-isopropylamino-s-triazine) is a water-soluble herbicide used extensively across the United States. Atrazine’s toxicity and persistent mobility directly affects the health of aquatic communities and poses serious downstream concerns for human health. Triazine hydrolase (TrzN) from <i>Arthrobacter aurescens</i> TC1, is an enzyme that catalytically degrades atrazine to the less toxic hydroxyatrazine product. We recognize TrzN’s potential as a biocatalyst and hypothesize that engineering solid support materials to immobilize TrzN will increase the breadth of its reactivity, thermal stability, and robustness necessary for developing a bioremediation process. To date, we have successfully immobilized TrzN in alginate beads (<b>Figure 1</b>). This TrzN:alginate biomaterial is catalytically active towards atrazine ~80% of the atrazine degraded after six hours. The process has &lt;1% protein loss during formation and no detectable protein loss during storage. The biocatalyst retained &gt;50% of its catalytic activity after being used once a week for 3 weeks. We have also successfully immobilized TrzN into sol-gel and zero-gel materials, which show promise to increase the stability of immobilized TrzN under more extreme reaction conditions such as temperature, pH, and organic solvents.

Immobilization of triazine hydrolase for atrazine bioremediation

ACS Spring 2022

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