Production and purification of a granular-starch-binding domain of glucoamylase 1 from Aspergillus niger

Nigel J. Belshaw, Gary Williamson

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50 Citations (Scopus)

Abstract

A domain of glucoamylase 1 from Aspergillus niger which binds to granular starch was produced by proteolytic digestion and purified to apparent homogeneity by extraction with corn starch followed by anion-exchange chromatography and gel filtration. The peptide has a molecular weight of 25100, contains approximately 38% carbohydrate ( w w) and corresponds to residues 471-616 at the C-terminus of glucoamylase 1. The peptide bound to granular corn starch maximally at 1.08 nmol mg starch. It inhibited the hydrolysis of granular starch by glucoamylase 1 but had no effect on the hydrolysis of starch in solution.

Original languageEnglish
Pages (from-to)350-353
Number of pages4
JournalFEBS Letters
Volume269
Issue number2
DOIs
Publication statusPublished - 3 Sep 1990
Externally publishedYes

Keywords

  • Aspergillus niger
  • Binding domain
  • Glucoamylase
  • Proteolysis
  • Starch binding

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