A novel organophosphate hydrolase from Arthrobacter sp. HM01: Characterization and applications.

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  • Additional Information
    • Source:
      Publisher: Elsevier Applied Science Country of Publication: England NLM ID: 9889523 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1873-2976 (Electronic) Linking ISSN: 09608524 NLM ISO Abbreviation: Bioresour Technol Subsets: MEDLINE
    • Publication Information:
      Original Publication: Barking, Essex, England : New York, N.Y. : Elsevier Applied Science ; Elsevier Science Pub. Co., 1991-
    • Subject Terms:
    • Abstract:
      Bioremediation systems coupled to efficient microbial enzymes have emerged as an attractive approach for the in-situ removal of hazardous organophosphates (OPs) pesticides from the polluted environment. However, the role of engineered enzymes in OPs-degradation is rarely studied. In this study, the potential OPs-hydrolase (opdH) gene (Arthrobacter sp. HM01) was isolated, cloned, expressed, and purified. The recombinant organophosphate hydrolase (ropdH) was ∼29 kDa; which catalyzed a broad-range of OPs-pesticides in organic-solvent (∼99 % in 30 min), and was found to increase the catalytic efficiency by 10-folds over the native enzyme (k cat /K m : 10 7 M -1 s -1 ). The degraded metabolites were analyzed using HPLC/GCMS. Through site-directed mutagenesis, it was confirmed that, conserved metal-bridged residue (Lys-127), plays a crucial role in OPs-degradation, which shows ∼18-folds decline in OPs-degradation. Furthermore, the catalytic activity and its stability has been enhanced by >2.0-fold through biochemical optimization. Thus, the study suggests that ropdH has all the required properties for OPs bioremediation.
      (Copyright © 2022 Elsevier Ltd. All rights reserved.)
    • Contributed Indexing:
      Keywords: Bioremediation; Chemical warfare agents; Organophosphorus; Pesticides; Phosphotriesterase; Site-directed mutagenesis
    • Accession Number:
      0 (HM01)
      0 (Organophosphorus Compounds)
      0 (Pesticides)
      0 (Piperidines)
      EC 3.1.3.- (phosphorylphosphatase)
      EC 3.1.3.2 (Phosphoric Monoester Hydrolases)
    • Publication Date:
      Date Created: 20220222 Date Completed: 20220314 Latest Revision: 20220314
    • Publication Date:
      20231215
    • Accession Number:
      10.1016/j.biortech.2022.126870
    • Accession Number:
      35192947