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

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).