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Detalle de: In Vivo Chaperone‐Assisted Folding of α ‐1,6‐Fucosyltransferase from Rhizobium sp.

Title In Vivo Chaperone‐Assisted Folding of α ‐1,6‐Fucosyltransferase from Rhizobium sp.
Abstract

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 Ni2+-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.

Apa Reference Bastida, A., Latorre, M. & García‐Junceda, E. (2003). In Vivo Chaperone‐Assisted Folding of α ‐1,6‐Fucosyltransferase from Rhizobium sp.. ChemBioChem, 4(6), 531-533. 10.1002/cbic.200200514
Doi 10.1002/cbic.200200514
Publication Date 2 Jun 2003
Publication Type Article
Researcher Agatha Bastida
Ontology
Research Groups
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