Improving storage stability of recombinant organophosphorus hydrolase

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

DOI: 10.1016/J.PEP.2015.01.012

关键词:

摘要: Abstract Organophosphorus hydrolase (OPH) is a ∼38 kDa enzyme encoded by opd gene of Flavobacterium sp. The can hydrolyze and inactivate variety organophosphate (OP)-compounds, including chemical warfare nerve agents. Thus, OPH strong candidate for the development therapeutic intervention against OP-poisoning in humans other animals. It also promising bio-decontaminating agent clean-up OP-contaminated objects areas. For successful commercial application, long-term storage stability purified important. In this study we have cloned expressed recombinant (r-OPH) Escherichia coli effect different excipients on was analyzed. stored either aqueous solution or lyophilized form at 25 °C 60 days presence absence determined monitoring paraoxon-hydrolyzing activity. Our results suggest that, (a) maltose, trehalose, arginine proline were most effective stabilizing when buffer 25 °C, (b) mannose exerted maximum stabilization 60 days. shows that common be used to stabilize order store it long period time under conditions. develop formulation(s) use.

参考文章(37)
Joseph J. DeFrank, William E. White, Phosphofluoridates: Biological Activity and Biodegradation Springer Berlin Heidelberg. pp. 295- 343 ,(2002) , 10.1007/10721878_10
Ma. Laura, Enrique Snchez-Salinas, Edgar Dantn Gonzlez, Mara Luisa, Pesticide Biodegradation: Mechanisms, Genetics and Strategies to Enhance the Process InTech. ,(2013) , 10.5772/56098
G.A. Omburo, J.M. Kuo, L.S. Mullins, F.M. Raushel, Characterization of the zinc binding site of bacterial phosphotriesterase. Journal of Biological Chemistry. ,vol. 267, pp. 13278- 13283 ,(1992) , 10.1016/S0021-9258(18)42207-7
Melinda E. Wales, Tony E. Reeves, Organophosphorus hydrolase as an in vivo catalytic nerve agent bioscavenger. Drug Testing and Analysis. ,vol. 4, pp. 271- 281 ,(2012) , 10.1002/DTA.381
Keith E. LeJeune, James R. Wild, Alan J. Russell, Nerve agents degraded by enzymatic foams Nature. ,vol. 395, pp. 27- 28 ,(1998) , 10.1038/25634
W W Mulbry, J S Karns, P C Kearney, J O Nelson, C S McDaniel, J R Wild, Identification of a plasmid-borne parathion hydrolase gene from Flavobacterium sp. by southern hybridization with opd from Pseudomonas diminuta. Applied and Environmental Microbiology. ,vol. 51, pp. 926- 930 ,(1986) , 10.1128/AEM.51.5.926-930.1986
Florian Nachon, Xavier Brazzolotto, Marie Trovaslet, Patrick Masson, Progress in the development of enzyme-based nerve agent bioscavengers ☆ Chemico-Biological Interactions. ,vol. 206, pp. 536- 544 ,(2013) , 10.1016/J.CBI.2013.06.012
Miguel Alcalde, Manuel Ferrer, Francisco J. Plou, Antonio Ballesteros, Environmental biocatalysis: from remediation with enzymes to novel green processes Trends in Biotechnology. ,vol. 24, pp. 281- 287 ,(2006) , 10.1016/J.TIBTECH.2006.04.002
Mark Cornell Manning, Danny K. Chou, Brian M. Murphy, Robert W. Payne, Derrick S. Katayama, Stability of Protein Pharmaceuticals: An Update Pharmaceutical Research. ,vol. 27, pp. 544- 575 ,(2010) , 10.1007/S11095-009-0045-6