Enhancing organophosphate hydrolase efficacy via protein engineering and immobilization strategies

Abstract

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.

Highly Sensitive and Rapid Screening Technique for the Detection of Organophosphate Pesticides and Copper Compounds Using Bifunctional Recombinant TrxA-PvCarE1

“…Organophosphate pesticides (OPs) have gained wide use in agriculture because they can effectively control various pests and enhance crop yields. 1,2 However, the presence of these chemicals and their metabolites in the food chain and associated biological enrichment pathways leads to their accumulation in humans and livestock, thereby posing potential health risks and toxic effects. 3,4 In organisms, OPs inhibit the activity of acetylcholinesterase (AChE), a crucial enzyme that is responsible for regulating neurotransmitters in the nervous system.…”

“…Organophosphate pesticides (OPs) have gained wide use in agriculture because they can effectively control various pests and enhance crop yields. , However, the presence of these chemicals and their metabolites in the food chain and associated biological enrichment pathways leads to their accumulation in humans and livestock, thereby posing potential health risks and toxic effects. , In organisms, OPs inhibit the activity of acetylcholinesterase (AChE), a crucial enzyme that is responsible for regulating neurotransmitters in the nervous system. This inhibition causes the accumulation of acetylcholine, resulting in neurotoxic symptoms and, in severe cases, even fatalities. , Similar to OPs, copper compounds have been commonly employed as fungicides and bactericides in agriculture for many years due to their broad spectrum of bactericidal properties, long-lasting effects, and cost-effectiveness .…”

Mesoporous Polymeric Ionic Liquid via Confined Polymerization for Laccase Immobilization towards Efficient Degradation of Phenolic Pollutants

“…However, in practice, protein engineering still faces many challenges. After protein modification, laccases exhibit unstable properties with regard to their preservation and application [ 14 ]. Both the covalent modification and non-covalent modification of enzyme systems are unstable, and the activity and stability of enzymes may be reduced after modification.…”

“…One of the significant advantages of enzyme immobilization is that it provides an expected ideal enzyme system that can be reused for a couple of cycles, reducing operation costs [ 11 , 17 ]. Currently, enzyme immobilization strategies mainly focus on supports innovation through the use of metallic compounds [ 18 ], carbon-based materials [ 19 ], silicon-based nanomaterials [ 20 ], metal-organic frameworks or their derivatives [ 14 ], polymers [ 21 ], etc. Liu and co-workers immobilized laccase into carbon-based mesoporous magnetic composites through adsorption.…”

Carrier Variety Used in Immobilization of His6-OPH Extends Its Application Areas

“…The improved biocatalytic characteristics and altered stereospecificity of the catalytic action were also revealed for the His 6 -OPH as compared to OPH [ 17 ]. The latter property can be achieved by combining the genetic introduction of a polyhistidine sequence into the enzyme molecule with site-directed mutations in the active center of the enzyme and in the amino acid residues around it or in the substrate-binding domain [ 11 , 18 ].…”