Ahn_2004_Chem.Commun.(Camb)__364

Reference

Title : Probing lipase\/esterase libraries for lipid A hydrolases--discovery of biocatalysts for the detoxification of bacterially-expressed recombinant protein - Ahn_2004_Chem.Commun.(Camb)__364
Author(s) : Ahn JM , Wentworth P, Jr. , Janda KD
Ref : Chem Commun (Camb) , :364 , 2004
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).

PubMedSearch : Ahn_2004_Chem.Commun.(Camb)__364
PubMedID: 14765210

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Citations formats

Ahn JM, Wentworth P, Jr., Janda KD (2004)
Probing lipase\/esterase libraries for lipid A hydrolases--discovery of biocatalysts for the detoxification of bacterially-expressed recombinant protein
Chem Commun (Camb) :364

Ahn JM, Wentworth P, Jr., Janda KD (2004)
Chem Commun (Camb) :364