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

Research output: Contribution to journal › Article › Research › 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 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	https://doi.org/10.1016/0014-5793(90)81191-P
Publication status	Published - 3 Sept 1990
Externally published	Yes

Keywords

Aspergillus niger
Binding domain
Glucoamylase
Proteolysis
Starch binding

Access to Document

10.1016/0014-5793(90)81191-P

Cite this

@article{cbe04f41831a4401b5c9fed413936ece,

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 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.",

keywords = "Aspergillus niger, Binding domain, Glucoamylase, Proteolysis, Starch binding",

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

year = "1990",

month = sep,

day = "3",

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

language = "English",

volume = "269",

pages = "350--353",

journal = "FEBS Letters",

issn = "0014-5793",

publisher = "John Wiley & Sons",

number = "2",

}

TY - JOUR

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 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.

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 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.

KW - Aspergillus niger

KW - Binding domain

KW - Glucoamylase

KW - Proteolysis

KW - Starch binding

UR - http://www.scopus.com/inward/record.url?scp=0025083002&partnerID=8YFLogxK

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

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

M3 - Article

C2 - 2119316

AN - SCOPUS:0025083002

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

Access to Document

Other files and links

Cite this