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Production and Purification of a Granular-Starch-Binding Domain of Glucoamylase 1 From Aspergillus Niger

N J Belshaw, G Williamson

FEBS Lett. 1990 Sep 3;269(2):350-3.

PMID: 2119316

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 25,100, 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.

Chemicals Related in the Paper:

Catalog Number Product Name Structure CAS Number Price
AP9032080-B Amyloglucosidase solution from Aspergillus niger Amyloglucosidase solution from Aspergillus niger 9032-08-0 Price
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