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A cellulose-binding module of the Trichoderma reesei @b-mannanase Man5A increases the mannan-hydrolysis of complex substrates

  • Per Hägglund
  • Torny Eriksson
  • Anna Collén
  • Wim Nerinckx
  • Marc Claeyssens
  • Henrik Stålbrand
Publiceringsår: 2003
Språk: Engelska
Sidor: 37-48
Publikation/Tidskrift/Serie: Journal of Biotechnology
Volym: 101
Nummer: 1
Dokumenttyp: Artikel i tidskrift
Förlag: Elsevier


Endo-@b-1,4-d-mannanases (@b-mannanase; EC are endohydrolases that participate in the degradation of hemicellulose, which is closely associated with cellulose in plant cell walls. The @b-mannanase from Trichoderma reesei (Man5A) is composed of an N-terminal catalytic module and a C-terminal carbohydrate-binding module (CBM). In order to study the properties of the CBM, a construct encoding a mutant of Man5A lacking the part encoding the CBM (Man5A@DCBM), was expressed in T. reesei under the regulation of the Aspergillus nidulans gpdA promoter. The wild-type enzyme was expressed in the same way and both proteins were purified to electrophoretic homogeneity using ion-exchange chromatography. Both enzymes hydrolysed mannopentaose, soluble locust bean gum galactomannan and insoluble ivory nut mannan with similar rates. With a mannan/cellulose complex, however, the deletion mutant lacking the CBM showed a significant decrease in hydrolysis. Binding experiments using activity detection of Man5A and Man5A@DCBM suggests that the CBM binds to cellulose but not to mannan. Moreover, the binding of Man5A to cellulose was compared with that of an endoglucanase (Cel7B) from T. reesei.


  • Biological Sciences
  • Carbohydrate-binding module
  • Hemicellulase
  • Cellulose
  • Hemicellulose
  • Endoglucanase


  • ISSN: 1873-4863

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