Journal Article

FZJ-2020-04381

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Small Angle Neutron Scattering Reveals Dimeric Glucose Oxidase from Aspergillus niger at pH 5.9

Erhan, R. V. (Corresponding author) ; Bodnarchuk, V. ; Radulescu, A.FZJ* ; Anghel, L. (Corresponding author)

2020
Springer Science+Business Media Berlin

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Please use a persistent id in citations: http://hdl.handle.net/2128/26292  doi:10.1134/S1027451020070125

Abstract: 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.

Keyword(s): Polymers, Soft Nano Particles and Proteins (1st) ; Biology (2nd)

Note: Bitte Post-print ergänzen

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Contributing Institute(s):

1. Neutronenstreuung (JCNS-1)
2. JCNS-FRM-II (JCNS-FRM-II)
3. Heinz Maier-Leibnitz Zentrum (MLZ)

Research Program(s):

1. 6G4 - Jülich Centre for Neutron Research (JCNS) (POF3-623) (POF3-623)
2. 6G15 - FRM II / MLZ (POF3-6G15) (POF3-6G15)

Experiment(s):

1. KWS-2: Small angle scattering diffractometer (NL3ao)

Appears in the scientific report 2020

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Database coverage:
; Clarivate Analytics Master Journal List ; DEAL Springer ; Emerging Sources Citation Index ; SCOPUS ; Web of Science Core Collection

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