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

Nigel J. Belshaw; Gary Williamson

doi:10.1016/0014-5793(90)81191-p

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

Nigel J. Belshaw
, Gary Williamson

School of Biological Sciences

Research output: Contribution to journal › Article › peer-review

53 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 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.

Original language	English
Pages (from-to)	350-353
Number of pages	4
Journal	FEBS Letters
Volume	269
Issue number	2
DOIs	https://doi.org/10.1016/0014-5793(90)81191-p
Publication status	Published - 03 Sept 1990

Keywords

Aspergillus Aspergillus niger

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title = "Production and purification of a granular-starch-binding domain of glucoamylase 1 from Aspergillus niger",

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.",

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author = "Belshaw, \{Nigel J.\} and Gary Williamson",

year = "1990",

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doi = "10.1016/0014-5793(90)81191-p",

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T1 - Production and purification of a granular-starch-binding domain of glucoamylase 1 from Aspergillus niger

AU - Belshaw, Nigel J.

AU - Williamson, Gary

PY - 1990/9/3

Y1 - 1990/9/3

N2 - 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.

AB - 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.

KW - Aspergillus Aspergillus niger

U2 - 10.1016/0014-5793(90)81191-p

DO - 10.1016/0014-5793(90)81191-p

M3 - Article

SN - 0014-5793

VL - 269

SP - 350

EP - 353

JO - FEBS Letters

JF - FEBS Letters

IS - 2

ER -

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

Abstract

Keywords

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