Novel xylan-binding properties of an engineered family 4 carbohydrate-binding module

Lavinia Cicortas Gunnarsson, Cedric Montanier, Richard B. Tunnicliffe, Mike R. Williamson, Harry J. Gilbert, Eva Nordberg Karlsson, Mats Ohlin

Research output: Contribution to journalArticlepeer-review


Molecular engineering of ligand-binding proteins is commonly used for identification of variants that display novel specificities. Using this approach to introduce novel specificities into CBMs (carbohydrate-binding modules) has not been extensively explored. Here, we report the engineering of a CBM, CBM42 from the Rhodothermits marinus xylanase Xyn10A, and the identification of the X-2 variant. As compared with the wildtype protein, this engineered module displays higher specificity for the polysaccharide xylan, and a lower preference for binding xylo-oligomers rather than binding the natural decorated polysaccharide. The mode of binding of X-2 differs from other xylan-specific CBMs in that it only has one aromatic residue in the binding site that can make hydrophobic interactions with the sugar rings of the ligand. The evolution of CBM4-2 has thus generated a xylan-binding module with different binding properties to those displayed by CBMs available in Nature.
Original languageEnglish
Pages (from-to)209-214
JournalBiochemical Journal
Publication statusPublished - 2007

Subject classification (UKÄ)

  • Biochemistry and Molecular Biology

Free keywords

  • thermodynamics
  • molecular engineering
  • carbohydrate-binding module
  • aromatic residue
  • binding specificity
  • xylan


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