Enhancing organophosphate hydrolase efficacy via protein engineering and immobilization strategies

Priya Katyal, Stanley Chu, Jin Kim Montclare

Research output: Contribution to journalReview articlepeer-review


Organophosphorus compounds (OPs), developed as pesticides and chemical warfare agents, are extremely toxic chemicals that pose a public health risk. Of the different detoxification strategies, organophosphate-hydrolyzing enzymes have attracted much attention, providing a potential route for detoxifying those exposed to OPs. Phosphotriesterase (PTE), also known as organophosphate hydrolase (OPH), is one such enzyme that has been extensively studied as a catalytic bioscavenger. In this review, we will discuss the protein engineering of PTE aimed toward improving the activity and stability of the enzyme. In order to make enzyme utilization in OP detoxification more favorable, enzyme immobilization provides an effective means to increase enzyme activity and stability. Here, we present several such strategies that enhance the storage and operational stability of PTE/OPH.

Original languageEnglish (US)
Pages (from-to)54-72
Number of pages19
JournalAnnals of the New York Academy of Sciences
Issue number1
StatePublished - Nov 17 2020


  • chemical warfare agents
  • organophosphate hydrolase
  • organophosphates
  • organophosphorus compounds
  • pesticides
  • phosphotriesterase

ASJC Scopus subject areas

  • General Neuroscience
  • General Biochemistry, Genetics and Molecular Biology
  • History and Philosophy of Science


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