This title appears in the Scientific Report :
2020
Please use the identifier:
http://hdl.handle.net/2128/26292 in citations.
Please use the identifier: http://dx.doi.org/10.1134/S1027451020070125 in citations.
Small Angle Neutron Scattering Reveals Dimeric Glucose Oxidase from Aspergillus niger at pH 5.9
Small Angle Neutron Scattering Reveals Dimeric Glucose Oxidase from Aspergillus niger at pH 5.9
Glucose oxidase (GOx) is a 160 kDa flavoenzyme dimer belonging to the family of glucose-methanol-choline oxidoreductases. Despite the abundant availability of information regarding the structure and mechanisms of interactions of GOx, there is still considerable interest in studying the properties of...
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Personal Name(s): | Erhan, R. V. (Corresponding author) |
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Bodnarchuk, V. / Radulescu, Aurel / Anghel, L. (Corresponding author) | |
Contributing Institute: |
Heinz Maier-Leibnitz Zentrum; MLZ JCNS-FRM-II; JCNS-FRM-II Neutronenstreuung; JCNS-1 |
Published in: | Journal of surface investigation, 14 (2020) S1, S. S5 - S10 |
Imprint: |
Berlin
Springer Science+Business Media
2020
|
DOI: |
10.1134/S1027451020070125 |
Document Type: |
Journal Article |
Research Program: |
FRM II / MLZ Jülich Centre for Neutron Research (JCNS) |
Subject (ZB): | |
Link: |
Restricted OpenAccess |
Publikationsportal JuSER |
Please use the identifier: http://dx.doi.org/10.1134/S1027451020070125 in citations.
Glucose oxidase (GOx) is a 160 kDa flavoenzyme dimer belonging to the family of glucose-methanol-choline oxidoreductases. Despite the abundant availability of information regarding the structure and mechanisms of interactions of GOx, there is still considerable interest in studying the properties of this protein to extend its bio-applications. The present study aims at investigating the conformational stability of GOx from Aspergillus niger in the optimal environment that presumably preserves its functional properties using small angle neutron scattering method. This method allowed computing the low-resolution three-dimensional models of the protein. Obtained results indicate protein dimerization in buffer solution pH 5.9, with a maximum particle dimension, Dmax, of 110 Å and Rg of 34.50 ± 0.025 Å. |