Covalent immobilization of organophosphorus hydrolase enzyme on chemically modified cellulose microfibers: Statistical optimization and characterization

Sharifi, Meisam; Robatjazi, Seyed Morteza; Sadri, Minoo; Mosaabadi, Jafar Mohammadian

doi:10.1016/j.reactfunctpolym.2018.01.019

Cited by 27 publications

(11 citation statements)

References 44 publications

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“…Therefore, the decreased activity of OpdA@Ni-NTA-VMSN might be ascribed to inactivation of the enzyme during the continuous use in the flow system, rather than the enzyme leaching from the Ni-NTA-VMSN . Sharifi et al also reported that hydrolysis reaction products on the active site and the frequent encountering between the immobilized OPH and substrate could result in the active site distortion and molecular denaturation of the enzyme …”

Section: Resultsmentioning

confidence: 99%

“…Organophosphates (OPs) are widely used as effective components in agricultural pesticides and insecticides owing to their extreme toxicity. , However, it is difficult to remove the residual OPs in the environment because of their high half-life and stability, which can lead to the ever-present contamination of environment and threats to human health . Therefore, a number of approaches have been developed for effective decontamination and detoxification of OPs.…”

Section: Introductionmentioning

confidence: 99%

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Facile Oriented Immobilization and Purification of His-Tagged Organophosphohydrolase on Viruslike Mesoporous Silica Nanoparticles for Organophosphate Bioremediation

Zhou

Gao

et al. 2018

ACS Sustainable Chem. Eng.

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In this study, nickel-nitrilotriacetic acid-modified viruslike mesoporous silica nanoparticles (Ni-NTA-VMSN) were fabricated by a facile method for the first time. The Ni2+ ions on the surface of Ni-NTA-VMSN provided abundant anchoring sites for directly selective oriented immobilization of His-tagged proteins from crude enzymes. By incubation of the Ni-NTA-VMSN in the His-tagged organophosphohydrolase (OpdA)-contained cell lysates, a nanobiocatalyst, OpdA@Ni-NTA-VMSN, could be constructed. At the optimal immobilization conditions, the specific activity of OpdA@Ni-NTA-VMSN was 353.0 U/gprotein, which was slightly higher than that of free OpdA in cell lysates. The substrate’s affinity capacity of OpdA became higher after oriented immobilization, and the OpdA@Ni-NTA-VMSN exhibited excellent catalytic activity and stability. In addition, when OpdA@Ni-NTA-VMSN was applied in a plug-flow reactor, the degradation percent of methyl parathion could be maintained at more than 90% with the injection of 20 mL of reaction mixture. Thus, the Ni-NTA-VMSN will be a promising material for purifying and immobilizing His-tagged enzymes. The proposed OpdA@Ni-NTA-VMSN will be an excellent nanobiocatalyst for biodegradation of organophosphorus pesticides.

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Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Facile Oriented Immobilization and Purification of His-Tagged Organophosphohydrolase on Viruslike Mesoporous Silica Nanoparticles for Organophosphate Bioremediation

Zhou

Gao

et al. 2018

ACS Sustainable Chem. Eng.

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“…Even with such reduced activities, immobilized PTE has been shown to hydrolyze dilute solutions of paraoxon or ethyl parathion and attain partial hydrolysis of DFP. 90 Several other substrates, including cellulose microfibers, 91 chitosan beads, 92 quantum dots, 93 carbon nanotubes, 94 gold NPs, 95 and agarose beds, 90 have been utilized to immobilize OPH. Some of these substrates are best suited for fabricating novel biosensors for OP detection and are discussed elsewhere.…”

Section: Stabilization/immobilization Strategiesmentioning

confidence: 99%

“…Several other substrates, including cellulose microfibers, 91 chitosan beads, 92 quantum dots, 93 carbon nanotubes, 94 gold NPs, 95 and agarose beds, 90 have been utilized to immobilize OPH. Some of these substrates are best suited for fabricating novel biosensors for OP detection and are discussed elsewhere 2,96 .…”

Section: Stabilization/immobilization Strategiesmentioning

confidence: 99%

Enhancing organophosphate hydrolase efficacy via protein engineering and immobilization strategies

Katyal

Chu

Montclare

2020

Annals of the New York Academy of Sciences

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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.

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“…For these purposes, many enzymes have been immobilized using different protocols, such as adsorption, covalent attachment, chemical aggregation, microencapsulation, and entrapment (Sun et al, 2010;Sharifi et al, 2018). In addition to the immobilization technique, selection of support material is also of vital importance for enzyme immobilization.…”

Section: Introductionmentioning

confidence: 99%

STABILIZATION STUDY OF TETRAMERIC Kluyveromyces lactis β-GALACTOSIDASE BY IMMOBILIZATION ON IMMOBEAD: THERMAL, PHYSICO-CHEMICAL, TEXTURAL AND CATALYTIC PROPERTIES

Gennari

Mobayed

Rafael

et al. 2019

Braz. J. Chem. Eng.

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Covalent immobilization of organophosphorus hydrolase enzyme on chemically modified cellulose microfibers: Statistical optimization and characterization

Cited by 27 publications

References 44 publications

Facile Oriented Immobilization and Purification of His-Tagged Organophosphohydrolase on Viruslike Mesoporous Silica Nanoparticles for Organophosphate Bioremediation

Facile Oriented Immobilization and Purification of His-Tagged Organophosphohydrolase on Viruslike Mesoporous Silica Nanoparticles for Organophosphate Bioremediation

Enhancing organophosphate hydrolase efficacy via protein engineering and immobilization strategies

STABILIZATION STUDY OF TETRAMERIC Kluyveromyces lactis β-GALACTOSIDASE BY IMMOBILIZATION ON IMMOBEAD: THERMAL, PHYSICO-CHEMICAL, TEXTURAL AND CATALYTIC PROPERTIES

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