Improving storage stability of recombinant organophosphorus hydrolase

Iyengar, A.R. Satvik; Tripathy, Rajan K.; Bajaj, Priyanka; Pande, Abhay H.

doi:10.1016/j.pep.2015.01.012

Cited by 10 publications

(2 citation statements)

References 35 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Iyengar et al . have screened a panel of excipients that can stabilize OPH (derived from Flavanobacterium) under aqueous and lyophilized conditions at 25 °C 56 . Of all the excipients, maltose, trehalose, proline, and arginine were the most effective stabilizers of OPH when stored under aqueous conditions.…”

Section: Stabilization/immobilization Strategiesmentioning

confidence: 99%

See 1 more Smart Citation

Enhancing organophosphate hydrolase efficacy via protein engineering and immobilization strategies

Katyal

Chu

Montclare

2020

Annals of the New York Academy of Sciences

View full text Add to dashboard Cite

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.

show abstract

Section: Stabilization/immobilization Strategiesmentioning

confidence: 99%

“…While freeze‐drying of OPH decreased its activity by 20%, addition of sugars (maltose, trehalose, and mannose) during lyophilization preserved its paraoxon‐hydrolyzing abilities and improved its stability for 2 months at 25 °C (Table 4). 56 …”

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

View full text Add to dashboard Cite

show abstract

Organophosphate-Hydrolyzing Enzymes as First-Line of Defence Against Nerve Agent-Poisoning: Perspectives and the Road Ahead

Iyengar

Pande

2016

Protein J

View full text Add to dashboard Cite

Nerve agents (NAs) are extremely neurotoxic synthetic organophosphate (OP) compounds exploited as weapons of mass destruction in terrorist attacks and chemical warfare. Considering the current world scenario, there is a persistent threat of NA-exposure to military personals and civilians. Various prophylactic and post-exposure treatments (such as atropine and oximes) available currently for NA-poisoning are inadequate and unsatisfactory and suffer from severe limitations. Hence, developing safe and effective treatment(s) against NA-poisoning is a critical necessity. With regards to counteracting NA-toxicity, the OP-hydrolyzing enzymes (OPHEs), which can hydrolyze and inactivate a variety of NAs, have emerged as promising candidates for the development of prophylactic therapy against NA-poisoning. However, there are many hurdles to be crossed before these enzymes can be brought to therapeutic use in humans. In this article, we have reviewed the various advancements in the field of development of OPHEs as prophylactic against NA-poisoning. The article majorly focuses on the toxic effects of NAs, various available therapies to counteract NA poisoning, the current status of OPHEs and attempts made to improve the various properties of these enzymes. Further, we have also briefly discussed about the prospective work that is needed to be undertaken for developing these OPHEs into those suitable for use in humans.

show abstract

Antibiotic-free expression system for the production of human interferon-beta protein

et al. 2017

Self Cite

View full text Add to dashboard Cite

Recombinant human interferon-β (rhIFN-β), a therapeutic protein, is produced using both prokaryotic and eukaryotic expression systems. However, instability of recombinant plasmid during cultivation of results in low yield of the recombinant proteins. In addition, use of antibiotics during the cultivation imposes a major concern. In this study, we have compared the expression yield of rhIFN-β in BL21 (DE3) and SE1 cells. Gene-encoding rhIFN-β was expressed in BL21 (DE3) and SE1 cells and the cultivation of recombinant cells was done in a laboratory scale bioreactor. Our results suggest that, compared to BL21(DE3) cells, the SE1 cells expressing rhIFN-β protein can be cultivated in the medium without antibiotic and provide increased stability of recombinant plasmid and higher expression yield of rhIFN-β protein. This system can be used for the production of rhIFN-β proteins for biomedical applications.

show abstract

Improving storage stability of recombinant organophosphorus hydrolase

Cited by 10 publications

References 35 publications

Enhancing organophosphate hydrolase efficacy via protein engineering and immobilization strategies

Enhancing organophosphate hydrolase efficacy via protein engineering and immobilization strategies

Organophosphate-Hydrolyzing Enzymes as First-Line of Defence Against Nerve Agent-Poisoning: Perspectives and the Road Ahead

Antibiotic-free expression system for the production of human interferon-beta protein

Contact Info

Product

Resources

About