Applied Microbiology and Biotechnology

, Volume 85, Issue 5, pp 1241–1249

Carbohydrate-binding domains: multiplicity of biological roles

  • Daniel Guillén
  • Sergio Sánchez
  • Romina Rodríguez-Sanoja
Mini-Review

DOI: 10.1007/s00253-009-2331-y

Cite this article as:
Guillén, D., Sánchez, S. & Rodríguez-Sanoja, R. Appl Microbiol Biotechnol (2010) 85: 1241. doi:10.1007/s00253-009-2331-y

Abstract

Insoluble polysaccharides can be degraded by a set of hydrolytic enzymes formed by catalytic modules appended to one or more non-catalytic carbohydrate-binding modules (CBM). The most recognized function of these auxiliary domains is to bind polysaccharides, bringing the biocatalyst into close and prolonged vicinity with its substrate, allowing carbohydrate hydrolysis. Examples of insoluble polysaccharides recognized by these enzymes include cellulose, chitin, β-glucans, starch, glycogen, inulin, pullulan, and xylan. Based on their amino acid similarity, CBMs are grouped into 55 families that show notable variation in substrate specificity; as a result, their biological functions are miscellaneous. Carbohydrate or polysaccharide recognition by CBMs is an important event for processes related to metabolism, pathogen defense, polysaccharide biosynthesis, virulence, plant development, etc. Understanding of the CBMs properties and mechanisms in ligand binding is of vital significance for the development of new carbohydrate-recognition technologies and provide the basis for fine manipulation of the carbohydrate–CBM interactions.

Keywords

Carbohydrate-binding domainsCarbohydrate-active proteinsGlucoside hydrolasesCarbohydrate targetingExpansinsLectins

Copyright information

© Springer-Verlag 2009

Authors and Affiliations

  • Daniel Guillén
    • 1
  • Sergio Sánchez
    • 1
  • Romina Rodríguez-Sanoja
    • 1
  1. 1.Departamento de Biología Molecular y Biotecnología del Instituto de Investigaciones BiomédicasUniversidad Nacional Autónoma de MéxicoMexicoMexico