Abstract:
: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 Pseudomonas syringae 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 p-nitrophenol (PNP) degrader, Pseudomonas putida 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 P. putida 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.
journal_name
Biotechnol Bioengjournal_title
Biotechnology and bioengineeringauthors
Yang C,Cai N,Dong M,Jiang H,Li J,Qiao C,Mulchandani A,Chen Wdoi
10.1002/bit.21535subject
Has Abstractpub_date
2008-01-01 00:00:00pages
30-7issue
1eissn
0006-3592issn
1097-0290journal_volume
99pub_type
杂志文章abstract::Measurement of the surface roughness and thickness of biological films is laborious and usually destructive, thus hampering research in this area. We developed a laser triangulation sensor (LTS) set-up for the fast and nondestructive measurement of these biofilm parameters during growth. Using LTS measurements, the mo...
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