Díaz M, Pedregosa A M, de Lucas J R, Torralba S, Monistrol I F, Laborda F
Departamento de Microbiología y Parasitología, Facultad de Farmacia, Universidad de Alcalá de Henares, Madrid, España.
Microbiologia. 1996 Dec;12(4):585-92.
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).
来自构巢曲霉菌丝体提取物的β-半乳糖苷酶已通过底物亲和色谱法纯化，并用于制备抗β-半乳糖苷酶多克隆抗体。以乳糖作为碳源生长的构巢曲霉合成一种活性形式的β-半乳糖苷酶，它似乎是一种450 kDa的多聚体酶，由120 kDa和97 kDa的单体组成。尽管该酶未释放到培养基中，但在细胞壁提取物中检测到了一些酶活性，因此表明它可能是一种胞外酶。构巢曲霉的β-半乳糖苷酶是一种非常不稳定的酶，最适pH值为7.5，最适温度为30℃。它仅对乳糖和对硝基苯基-β-D-半乳糖苷（PNPG）等β-半乳糖苷底物有活性。
