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Molecular engineering of a thermostable carbohydrate-binding module

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

Sammanfattning

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.

Disputation

Nyckelord

  • Technology and Engineering
  • Medicine and Health Sciences
  • carbohydrate-binding module
  • binding specificity
  • combinatorial
  • library
  • molecular engineering
  • phage-display
  • protein scaffold

Övriga

Sixth Carbohydrate Bioengineering Meeting
2014-04-04
Barcelona, Spain
Published
Yes
  • ISSN: 1024-2422

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