PMID: 2119316Sep 3, 1990Paper

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

FEBS Letters
N J Belshaw, G Williamson

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.

References

Nov 1, 1989·Analytical Biochemistry·S C Gill, P H von Hippel
Feb 3, 1986·European Journal of Biochemistry·B SvenssonA Gunnarsson
Aug 1, 1961·The Biochemical Journal·G N WILKINSON

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Citations

Mar 19, 2013·Applied Microbiology and Biotechnology·D GuillénR Rodríguez-Sanoja
May 9, 2001·Biochimica Et Biophysica Acta·S L SlaughterP J Butterworth
Jul 15, 1992·European Journal of Biochemistry·G WilliamsonM P Williamson
Feb 1, 1993·European Journal of Biochemistry·N J Belshaw, G Williamson
Oct 1, 1994·European Journal of Biochemistry·B W SigurskjoldH Driguez
May 2, 1994·Annals of the New York Academy of Sciences·A R KusnadiC M Metzler
Jan 1, 1996·Annual Review of Microbiology·R A Warren
Jun 27, 2007·BMC Biochemistry·Shu-Chuan LinMargaret Dah-Tsyr Chang
Aug 28, 2009·Critical Reviews in Biotechnology·Pardeep Kumar, T Satyanarayana
Aug 18, 2009·The FEBS Journal·Camilla ChristiansenBirte Svensson
Apr 28, 1999·FEBS Letters·S M SouthallM P Williamson
Oct 3, 1999·Applied and Environmental Microbiology·K OhdanS Okada
Feb 6, 2002·Chembiochem : a European Journal of Chemical Biology·H Driguez
May 30, 1991·Biochimica Et Biophysica Acta·N J Belshaw, G Williamson

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