Production and purification of a granular‐starch‐binding domain of glucoamylase 1 from Aspergillus niger
- 3 September 1990
- journal article
- Published by Wiley in FEBS Letters
- Vol. 269 (2), 350-353
- https://doi.org/10.1016/0014-5793(90)81191-p
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 (ww) and corresponds to residues 471–616 at the C-terminus of glucoamylase 1. The peptide bound to granular corn starch maximally at 1.08 nmolmg starch. It inhibited the hydrolysis of granular starch by glucoamylase 1 but had no effect on the hydrolysis of starch in solutionKeywords
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