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

Jung Mo Ahn; Paul Wentworth; Kim D. Janda

doi:10.1039/b312662e

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

Jung Mo Ahn, Paul Wentworth, Kim D. Janda

Urology

Research output: Contribution to journal › Article › peer-review

9 Scopus citations

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).

Original language	English (US)
Pages (from-to)	364-365
Number of pages	2
Journal	Chemical Communications
Volume	4
Issue number	4
DOIs	https://doi.org/10.1039/b312662e
State	Published - Jan 1 2004

ASJC Scopus subject areas

Catalysis
Electronic, Optical and Magnetic Materials
Ceramics and Composites
Chemistry(all)
Surfaces, Coatings and Films
Metals and Alloys
Materials Chemistry

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

Abstract

ASJC Scopus subject areas

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