Intracellular and extracellular production of proteins in Aspergillus under the control of expression signals of the highly expressed Aspergillus nidulans gpdA gene

article
The expression in Aspergillus is described of genes, coding for intracellular and extracellular proteins controlled by the promoter region of the constitutively and efficiently expressed glyceraldehyde-3-phosphate dehydrogenase gene (gpdA) of Aspergillus nidulans. Both the homologous gpdA and the heterologous Escherichia coli β-galactosidase (lacZ) and β-glucuronidase (uidA) genes could be expressed intracellularly at levels as high as 10-25% of total soluble protein. Efficient extracellular production of A. niger glucoamylase could be achieved with a fusion-gene containing the region of the glucoamylase gene coding for the mature protein preceded by a synthetic fungal signal sequence. Extracellular production of a heterologous protein, E. coli β-glucuronidase, with such a fusion was much less efficient. Only very low levels of β-glucuronidase were detected in the culture fluid, whereas considerable enzyme activity was detected in the mycelium. Chemicals/CAS: Bacterial Proteins; beta-Galactosidase, EC 3.2.1.23; Fungal Proteins; Genetic Vectors; Glucan 1,4-alpha-Glucosidase, EC 3.2.1.3; Glucosephosphate Dehydrogenase, EC 1.1.1.49; Glucuronidase, EC 3.2.1.31; Recombinant Fusion Proteins
TNO Identifier
231448
ISSN
01681656
Source
Journal of Biotechnology, 17(1), pp. 19-33.
Pages
19-33
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