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

FEBS Letters

Belshaw, Nigel J.¹  Williamson, Gary¹ 

[1] AFRC Institute of Food Research, Colney Lane, Norwich, Norfolk, NR4 7VA, UK

关键词: Glucoamylase;    Binding domain;    Starch binding;    Proteolysis;    Aspergillus niger;    Gl;    glucoamylase 1;    G2;    glucoamylase 2;    G1C;    C-terminal granular-starch-binding domain from glucoamylase 1 (residues 471–616);   

DOI  :  10.1016/0014-5793(90)81191-P

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 () and corresponds to residues 471–616 at the C-terminus of glucoamylase 1. The peptide bound to granular corn starch maximally at 1.08 starch. It inhibited the hydrolysis of granular starch by glucoamylase 1 but had no effect on the hydrolysis of starch in solution.

【 授权许可】

Unknown