title: Purification and properties of beta-galactosidase from Aspergillus nidulans.
abstract: Beta-Galactosidase from mycelial extract of Aspergillus nidulans has been purified by substrate affinity chromatography and used to obtain anti-beta-galactosidase polyclonal antibodies. A. nidulans growing in lactose as carbon source synthesizes one active form of beta-galactosidase which seems to be a multimeric enzyme of 450 kDa composed of monomers with 120 and 97 kDa. Although the enzyme was not released to the culture medium, some enzymatic activity was detected in a cell-wall extract, thus suggesting that it can be an extracellular enzyme. Beta-Galactosidase of A. nidulans is a very unstable enzyme with an optimum pH value of 7.5 and an optimum temperature of 30 degrees C. It was only active against beta-galactoside substrates like lactose and p-nitrophenyl-beta-D-galactoside (PNPG).
authors.affiliation: Departamento de Microbiología y Parasitología, Facultad de Farmacia, Universidad de Alcalá de Henares, Madrid, España.
authors.forename: M
authors.initials: M
authors.lastname: Díaz
authors.forename: A M
authors.initials: AM
authors.lastname: Pedregosa
authors.forename: J R
authors.initials: JR
authors.lastname: de Lucas
authors.forename: S
authors.initials: S
authors.lastname: Torralba
authors.forename: I F
authors.initials: IF
authors.lastname: Monistrol
authors.forename: F
authors.initials: F
authors.lastname: Laborda
mesh_terms: D001233:Aspergillus nidulans / Q000201:enzymology*; D001616:beta-Galactosidase / Q000032:analysis / Q000302:isolation & purification*
chemical_list: D001616:beta-Galactosidase