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In Vivo Chaperone‐Assisted Folding of α ‐1,6‐Fucosyltransferase from Rhizobium sp.
Author(s) -
Bastida Agatha,
Latorre Montserrat,
GarcíaJunceda Eduardo
Publication year - 2003
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.200200514
Subject(s) - fucosyltransferase , chaperonin , groel , chaperone (clinical) , groes , chemistry , biochemistry , recombinant dna , agarose , enzyme , protein folding , escherichia coli , gene , medicine , pathology
Three is not a crowd : Coexpression of the chaperonins GroEL/GroES with the α ‐1,6‐fucosyltransferase from Rhizobium sp. allows a 10‐fold increase in production of soluble and active fucosyltransferase. The His‐tagged fucosyltransferase can be purified and immobilized on Ni 2+ ‐IDA‐agarose gel in only one step (see Scheme). The immobilization leads to an important stabilization of the recombinant enzyme, which allows the preparation of a robust biocatalyst for the synthesis of oligosaccharides.