AFM images of complexes between amylose and Aspergillus niger glucoamylase mutants, native and mutant starch binding domains: A model for the action of glucoamylase

Victor J. Morris, A. Patrick Gunning, Craig B. Faulds, Gary Williamson, Birte Svensson

Research output: Contribution to journalArticleResearchpeer-review

53 Citations (Scopus)


Atomic force microscopy has been used to investigate the complexes formed between high molecular weight amylose chains and Aspergillus niger glucoamylase mutants (E400Q and W52F), wild-type A. niger starch binding domains (SBDs), and mutant SBDs (W563K and W590K) lacking either of the two starch binding sites. The images are interpreted in terms of a favourable binding between the amylose chains and the wild-type SBDs, leading to the formation of ring-like structures, in which parallel strands of the amylose molecule bind to both binding sites on the SBDs. The SBDs are seen to form a template for the assembly of an expanded amylosic double helix. This model for amylose-SBD binding has been used to propose a molecular mechanism for the role of the SBD in the hydrolytic action of glucoamylase on starch granules. The SBDs are considered to recognise the ends of amylosic double helices formed by the short amylosic chains present as branches on the amylopectin molecules, and displayed on the face of crystalline lamellae. This allows the binding and immobilisation of chain ends by the SBD, facilitating binding and cleavage by the exo-acting catalytic domain.

Original languageEnglish
Pages (from-to)1-7
Number of pages7
Issue number1
Publication statusPublished - 1 Jan 2005
Externally publishedYes


  • Aspergillus niger
  • Atomic force microscopy
  • Glucoamylase
  • Starch-binding domain

Cite this