Residue-specific global fluorination of Candida antarctica lipase B in Pichia pastoris
29.04.2010
Budisa N, Wenger W, Wiltschi B
Mol Biosyst. 6(9):1630-9
In Pichia pastoris, the Trp, Tyr, and Phe residues of heterologously expressed Candida antarctica lipase B were replaced by 5-fluorotryptophan, meta-fluorotyrosine, or para-fluorophenylalanine, respectively. The fluorous variant proteins were active lipases, though their catalytic activity was lower than that of the non-fluorinated parent protein. Importantly, we observed that the global fluorination prolonged the shelf life of the lipase activity, which is an especially useful feature for the storage of, e.g., therapeutic.
