Article
Assessment of immobilized PGA orientation via the LC-MS analysis of tryptic digests of the wild type and its 3K-PGA mutant assists in the rational design of a high-performance biocatalyst.
Analytical and bioanalytical chemistry - 1 Jan 2013
Serra Immacolata, Ubiali Daniela, Cecchini Davide A, Calleri Enrica, Albertini Alessandra M, Terreni Marco, Temporini Caterina
Abstract excerpt
The mutant penicillin G acylase (PGA) 3K-PGA contains three additional Lys residues on the surface opposite the active site. This protein was designed to selectively drive its immobilization on aldehyde supports. We describe here a modified bottom-up proteomic method to assess the orientation of the immobilized wild-type and mutant proteins to verify our hypothesis of a driven immobilization induced by the...
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