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

Nathalie Juge, Marie-Francoise Le Gal-Coëffet, Caroline S. M. Furniss, A. Patrick Gunning, Birte Kramhøft, Vic J. Morris, Birte Svensson, Gary Williamson

Research output: Contribution to journalConference articleResearchpeer-review

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 I 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.
Original languageEnglish
JournalBiologia
Volume57
Issue numbersuppl. 11
Pages (from-to)239-245
ISSN0006-3088
Publication statusPublished - 2002
Externally publishedYes
Event1st Symposium on the Alpha-Amylase Family - Smolenice Castle, Smolenice, Slovakia
Duration: 30 Sep 20014 Oct 2001

Conference

Conference1st Symposium on the Alpha-Amylase Family
LocationSmolenice Castle
CountrySlovakia
CitySmolenice
Period30/09/200104/10/2001

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