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000887724 1001_ $$0P:(DE-HGF)0$$aErhan, R. V.$$b0$$eCorresponding author
000887724 245__ $$aSmall Angle Neutron Scattering Reveals Dimeric Glucose Oxidase from Aspergillus niger at pH 5.9
000887724 260__ $$aBerlin$$bSpringer Science+Business Media$$c2020
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000887724 520__ $$aGlucose oxidase (GOx) is a 160 kDa flavoenzyme dimer belonging to the family of glucose-methanol-choline oxidoreductases. Despite the abundant availability of information regarding the structure and mechanisms of interactions of GOx, there is still considerable interest in studying the properties of this protein to extend its bio-applications. The present study aims at investigating the conformational stability of GOx from Aspergillus niger in the optimal environment that presumably preserves its functional properties using small angle neutron scattering method. This method allowed computing the low-resolution three-dimensional models of the protein. Obtained results indicate protein dimerization in buffer solution pH 5.9, with a maximum particle dimension, Dmax, of 110 Å and Rg of 34.50 ± 0.025 Å.
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000887724 7001_ $$0P:(DE-HGF)0$$aBodnarchuk, V.$$b1
000887724 7001_ $$0P:(DE-Juel1)130905$$aRadulescu, Aurel$$b2
000887724 7001_ $$0P:(DE-HGF)0$$aAnghel, L.$$b3$$eCorresponding author
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