Surface display of MPH on <i>Pseudomonas putida</i> JS444 using ice nucleation protein and its application in detoxification of organophosphates
書誌事項
- 公開日
- 2007-06-15
- 権利情報
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- http://onlinelibrary.wiley.com/termsAndConditions#vor
- DOI
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- 10.1002/bit.21535
- 公開者
- Wiley
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説明
<jats:title>Abstract</jats:title><jats:p>Methyl parathion hydrolase (MPH) has been displayed on the surface of microorganisms for the first time using only N‐ and C‐terminal domains of the ice nucleation protein (INPNC) from <jats:italic>Pseudomonas syringae</jats:italic> INA5 as an anchoring motif. A shuttle vector pINCM coding for INPNC–MPH was constructed and used to target MPH onto the surface of a natural <jats:italic>p</jats:italic>‐nitrophenol (PNP) degrader, <jats:italic>Pseudomonas putida</jats:italic> JS444, overcoming the potential substrate uptake limitation. Over 90% of the MPH activity was located on the cell surface as determined by protease accessibility and cell fractionation experiments. The surface localization of the INPNC–MPH fusion was further verified by Western blot analysis and immunofluorescence microscopy. The engineered <jats:italic>P. putida</jats:italic> JS444 degraded organophosphates as well as PNP rapidly without growth inhibition. Compared to organophosphorus hydrolase‐displaying systems reported, changes in substrate specificity highlight an important potential use of the engineered strain for the clean‐up of specific organophosphate nerve agents. Biotechnol. Bioeng. 2008;99: 30–37. © 2007 Wiley Periodicals, Inc.</jats:p>
収録刊行物
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- Biotechnology and Bioengineering
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Biotechnology and Bioengineering 99 (1), 30-37, 2007-06-15
Wiley