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Updated: Jul 12, 2026

Customization of Aspergillus niger Morphology Through Addition of Talc Micro Particles
Published on: March 15, 2012
Crystallization and preliminary X-ray diffraction data of β-galactosidase from Aspergillus niger
Agustín Rico-Díaz1, Ángel Vizoso Vázquez1, M Esperanza Cerdán1
1Grupo EXPRELA, Departamento de Bioloxía Celular e Molecular, Facultade de Ciencias, Universidade da Coruña, Campus da Zapateira, s/n, 15071 A Coruña, Spain.
Abstract:
β-Galactosidase from Aspergillus niger (An-β-Gal), belonging to the family 35 glycoside hydrolases, hydrolyzes the β-galactosidase linkages in lactose and other galactosides. It is extensively used in industry owing to its high hydrolytic activity and safety. The enzyme has been expressed in yeasts and purified by immobilized metal-ion affinity chromatography for crystallization experiments. The recombinant An-β-Gal, deglycosylated to avoid heterogeneity of the sample, has a molecular mass of 109 kDa. Rod-shaped crystals grew using PEG 3350 as the main precipitant agent. A diffraction data set was collected to 1.8 Å resolution.

