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 language | English |
|---|---|
| Pages (from-to) | 350-353 |
| Number of pages | 4 |
| Journal | FEBS Letters |
| Volume | 269 |
| Issue number | 2 |
| DOIs | |
| Publication status | Published - 3 Sep 1990 |
| Externally published | Yes |
Keywords
- Aspergillus niger
- Binding domain
- Glucoamylase
- Proteolysis
- Starch binding