Probing lipase/esterase libraries for lipid A hydrolases--discovery of biocatalysts for the detoxification of bacterially-expressed recombinant protein.
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).
Ahn
Jung-Mo
JM
Department of Chemistry, The Scripps Research Institute and the Skaggs Institute for Chemical Biology, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.
Wentworth
Paul
P
Janda
Kim D
KD
D000818:Animals; D000911:Antibodies, Monoclonal / Q000096:biosynthesis*; D002384:Catalysis; D003001:Cloning, Molecular; D004926:Escherichia coli / Q000378:metabolism*; D004950:Esterases / Q000737:chemistry*; D006868:Hydrolysis; D008049:Lipase / Q000737:chemistry; D008050:Lipid A / Q000737:chemistry* / Q000378:metabolism; D015335:Molecular Probes; D015202:Protein Engineering / Q000592:standards; D011994:Recombinant Proteins / Q000096:biosynthesis*
D000911:Antibodies, Monoclonal; D008050:Lipid A; D015335:Molecular Probes; D011994:Recombinant Proteins; D004950:Esterases; D008049:Lipase