Literature DB >> 2119316

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

N J Belshaw1, 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.

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Year:  1990        PMID： 2119316     DOI： 10.1016/0014-5793(90)81191-p

Source DB:  PubMed          Journal:  FEBS Lett        ISSN： 0014-5793            Impact factor:   4.124


  6 in total

1.  Alpha-amylase starch binding domains: cooperative effects of binding to starch granules of multiple tandemly arranged domains.

Authors:  D Guillén; M Santiago; L Linares; R Pérez; J Morlon; B Ruiz; S Sánchez; R Rodríguez-Sanoja
Journal:  Appl Environ Microbiol       Date:  2007-04-27       Impact factor: 4.792

2.  Characteristics of two forms of alpha-amylases and structural implication.

Authors:  K Ohdan; T Kuriki; H Kaneko; J Shimada; T Takada; Z Fujimoto; H Mizuno; S Okada
Journal:  Appl Environ Microbiol       Date:  1999-10       Impact factor: 4.792

3.  The family 21 carbohydrate-binding module of glucoamylase from Rhizopus oryzae consists of two sites playing distinct roles in ligand binding.

Authors:  Wei-I Chou; Tun-Wen Pai; Shi-Hwei Liu; Bor-Kai Hsiung; Margaret D-T Chang
Journal:  Biochem J       Date:  2006-06-15       Impact factor: 3.857

4.  Production, purification and characterization of the catalytic domain of glucoamylase from Aspergillus niger.

Authors:  B Stoffer; T P Frandsen; P K Busk; P Schneider; I Svendsen; B Svensson
Journal:  Biochem J       Date:  1993-05-15       Impact factor: 3.857

5.  O-glycosylation in Aspergillus glucoamylase. Conformation and role in binding.

Authors:  G Williamson; N J Belshaw; M P Williamson
Journal:  Biochem J       Date:  1992-03-01       Impact factor: 3.857

6.  Role of the linker region in the expression of Rhizopus oryzae glucoamylase.

Authors:  Shu-Chuan Lin; Wei-Ting Liu; Shi-Hwei Liu; Wei-I Chou; Bor-Kai Hsiung; I-Ping Lin; Chia-Chin Sheu; Margaret Dah-Tsyr Chang
Journal:  BMC Biochem       Date:  2007-06-25       Impact factor: 4.059
  6 in total

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