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Issue 4, 2004
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Probing lipase/esterase libraries for lipid A hydrolases—discovery of biocatalysts for the detoxification of bacterially-expressed recombinant protein

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Abstract

In our ongoing efforts to develop new methods for lipopolysaccharide (LPS) detoxification, we have screened lipase/esterase libraries for the ability to deacylate the 2′- and 3′-fatty acid chains from lipid A: the most active esterases were successfully employed to inactivate LPSs in a crude concentrated cell supernatant of E. Coli containing a recombinant single chain antibody (scFv).

Graphical abstract: Probing lipase/esterase libraries for lipid A hydrolases—discovery of biocatalysts for the detoxification of bacterially-expressed recombinant protein

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Publication details

The article was received on 10 Oct 2003, accepted on 19 Nov 2003 and first published on 19 Jan 2004


Article type: Communication
DOI: 10.1039/B312662E
Citation: Chem. Commun., 2004,0, 364-365

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    Probing lipase/esterase libraries for lipid A hydrolases—discovery of biocatalysts for the detoxification of bacterially-expressed recombinant protein

    J. Ahn, P. Wentworth, Jr. and K. D. Janda, Chem. Commun., 2004, 0, 364
    DOI: 10.1039/B312662E

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