Javascript verkar inte påslaget? - Vissa delar av Lunds universitets webbplats fungerar inte optimalt utan javascript, kontrollera din webbläsares inställningar.
Du är här

Molecular engineering of a thermostable carbohydrate-binding module

Publiceringsår: 2006
Språk: Engelska
Sidor: 31-37
Publikation/Tidskrift/Serie: Biocatalysis and Biotransformation
Volym: 24
Nummer: 1-2
Dokumenttyp: Konferensbidrag
Förlag: Taylor & Francis


Structure-function studies are frequently practiced on the very diverse group of natural carbohydrate-binding modules in order to understand the target recognition of these proteins. We have taken a step further in the study of carbohydrate-binding modules and created variants with novel binding properties by molecular engineering of one such molecule of known 3D-structure. A combinatorial library was created from the sequence encoding a thermostable carbohydrate-binding module, CBM4-2 from a Rhodothermus marinus xylanase, and phage-display technology was successfully used for selection of variants with specificity towards different carbohydrate polymers (birchwood xylan, Avicel (TM), ivory nut mannan and recently also xyloglucan), as well as towards a glycoprotein (human IgG4). Our work not only generated a number of binders with properties that would suite a range of biotechnological applications, but analysis of selected binders also helped us to identify residues important for their specificities.


  • Immunology in the medical area
  • Industrial Biotechnology
  • carbohydrate-binding module
  • binding specificity
  • combinatorial
  • library
  • molecular engineering
  • phage-display
  • protein scaffold


Sixth Carbohydrate Bioengineering Meeting
  • ISSN: 1029-2446
  • ISSN: 1024-2422

Box 117, 221 00 LUND
Telefon 046-222 00 00 (växel)
Telefax 046-222 47 20
lu [at] lu [dot] se

Fakturaadress: Box 188, 221 00 LUND
Organisationsnummer: 202100-3211
Om webbplatsen