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Molecular engineering of a thermostable carbohydrate-binding module

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Author

Summary, in English

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.

Publishing year

2006

Language

English

Pages

31-37

Publication/Series

Biocatalysis and Biotransformation

Volume

24

Issue

1-2

Document type

Conference paper

Publisher

Taylor & Francis

Topic

  • Immunology in the medical area
  • Industrial Biotechnology

Keywords

  • carbohydrate-binding module
  • binding specificity
  • combinatorial
  • library
  • molecular engineering
  • phage-display
  • protein scaffold

Conference name

Sixth Carbohydrate Bioengineering Meeting

Conference date

2005-04-03 - 2005-04-06

Conference place

Barcelona, Spain

Status

Published

Project

  • Designed carbohydrate binding modules and molecular probes

ISBN/ISSN/Other

  • ISSN: 1024-2422
  • ISSN: 1029-2446