Biologia, Bratislava, 57/Suppl. 11: 239-245, 2002.

ISSN 0006-3088 (Biologia).

 

Review

The starch binding domain of glucoamylase from Aspergillus niger: overview of its structure, function, and role in raw-starch hydrolysis.

 

Nathalie Juge1,2*, Marie-Francoise Le Gal-Coeffet1, Caroline S. M. Furniss1, A. Patrick Gunning1, Birte Kramhoft3, Vic J. Morris1, Gary Williamson1 & Birte Svensson3

1 Institute of Food Research, Norwich Research Park, Colney, Norwich, NR4 7UA, U.K.; tel.: ++ 44 1603 255068, fax: ++ 44 1603 255038, e-mail: nathalie.juge@bbsrc.ac.uk

2 Institut Méditerraneen de Recherche en Nutrition, UMR INRA 1111, Faculte des Sciences de St Jerome, Av. Escadrille Normandie-Niemen, Marseilles, F-13397 Cedex 20, France

3 Department of Chemistry, Carlsberg Laboratory, Gamle Carlsberg Vej 10, DK-2500 Copenhagen Valby, Denmark

* corresponding author

Received: October 26, 2001 / Accepted: March 20, 2002

 

Abstract

A carbohydrate-binding module is defined as a contiguous amino-acid sequence within a carbohydrate-active enzyme, with a discrete fold having carbohydrate-binding activity. Glucoamylase 1 from Aspergillus niger contains a C-terminal starch-binding domain (SBD), which is connected to the catalytic domain via a semi-rigid linker. Over the last 20 years, a combination of techniques (mutagenesis, nuclear magnetic resonance spectroscopy, differential scanning calorimetry, isothermal titration calorimetry, ultraviolet difference spectroscopy, atomic force microscopy, protein engineering) have been used to investigate the structure-function relationships of this particular domain. This review focuses on recent findings on the structure, role in ligand binding, cooperation in the hydrolysis of granular starch, and engineering of the A. niger glucoamylase SBD.

 

Key words: starch-binding domain, A. niger, glucoamylase, barley a-amylase, atomic force microscopy, raw-starch; fusion.