Interaction of β-cyclodextrin with the granular starch binding domain of glucoamylase

Nigel J. Belshaw, Gary Williamson

Research output: Contribution to journalArticleResearchpeer-review

36 Citations (Scopus)


The granular starch binding domain of glucoamyla 1 (EC 1,4-α-d-glucan glucohydrolase) binds two molecules of β-cyclodextrin, with a dissociation constant (Kd) for the second ligand of 1.68 μM. The catalytic domain showed no interaction with β-cyclodextrin. β-cyclodextrin competitively inhibited the adsorption of the binding domain onto granular starch with an inhibition constant (Ki) of 11.0 ± 1.9 μM. The results show that β-cyclodextrin binds to the binding domain of glucoamylase at the same site(s) as granular starch.

Original languageEnglish
Pages (from-to)117-120
Number of pages4
JournalBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
Issue number1
Publication statusPublished - 30 May 1991
Externally publishedYes


  • Binding domain
  • Cyclodextrin
  • Glucoamylase
  • Starch

Cite this