TY  - JOUR
AU  - Erhan, R. V.
AU  - Bodnarchuk, V.
AU  - Radulescu, Aurel
AU  - Anghel, L.
TI  - Small Angle Neutron Scattering Reveals Dimeric Glucose Oxidase from Aspergillus niger at pH 5.9
JO  - Journal of surface investigation
VL  - 14
IS  - S1
SN  - 1819-7094
CY  - Berlin
PB  - Springer Science+Business Media
M1  - FZJ-2020-04381
SP  - S5 - S10
PY  - 2020
N1  - Bitte Post-print ergänzen
AB  - 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.
LB  - PUB:(DE-HGF)16
UR  - <Go to ISI:>//WOS:000578828100002
DO  - DOI:10.1134/S1027451020070125
UR  - https://juser.fz-juelich.de/record/887724
ER  -