AFM Images of Complexes between Amylose andAspergillus niger Glucoamylase Mutants, Native and Mutant Starch Binding Domains: A Model for the Action of Glucoamylase-Reference-Cited by-同舟云学术

AFM Images of Complexes between Amylose andAspergillus niger Glucoamylase Mutants, Native and Mutant Starch Binding Domains: A Model for the Action of Glucoamylase

Published:2005-01 Issue:1 Volume:57 Page:1-7
ISSN:0038-9056
Container-title:STARCH - ST�RKE
language:en
Short-container-title:Starch - St�rke

Author:

Morris Victor J.,Gunning A. Patrick,Faulds Craig B.,Williamson Gary,Svensson Birte

Publisher

Wiley

Subject

Organic Chemistry,Food Science

Reference39 articles.

1. The complete amino acid sequence of the glycoprotein, glucoamylase G1, from Aspergillus niger

2. Characterization of a glucoamylase G2 from Aspergillus niger

3. Characterization of two forms of glucoamylase from aspergillus niger

4. Production and purification of a granular-starch-binding domain of glucoamylase 1 fromAspergillus niger

5. Activity and thermal stability of genetically truncated forms of Aspergillus glucoamylase

Cited by 50 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. A starch-binding domain of α-amylase (AmyPG) disrupts the structure of raw starch;International Journal of Biological Macromolecules;2024-02

2. Novel Design of an α-Amylase with an N-Terminal CBM20 in Aspergillus niger Improves Binding and Processing of a Broad Range of Starches;Molecules;2023-06-27

3. Diversity and biotechnological applications of microbial glucoamylases;Glycoside Hydrolases;2023

4. Starch-Binding Domain Modulates the Specificity of Maltopentaose Production at Moderate Temperatures;Journal of Agricultural and Food Chemistry;2022-07-13

5. Fusion of maltooligosaccharide-forming amylases from two origins for the improvement of maltopentaose synthesis;Food Research International;2021-12