Heterologous protein expression in filamentous fungi is advantageous, especially in the context of large scale production of high volume low value recombinant proteins. However, such systems are rare and not available in public domain. A novel filamentous fungus - Aspergillus unguis NII 08123 was used as host for developing a protein expression system. An expression cassette was assembled using A. nidulans glyceraldehyde 3 phosphate dehydrogenase promoter (Pgapd), tryptophan synthase transcription terminator (TtrpC) and hygromycin resistance gene (hph) as selection marker. The enhanced green fluorescent protein (GFP) gene from Aequorea victoria was used as the model test protein for the evaluation of the expression system. The genetic transformation of this novel fungus was optimized through electroporation. Use of heterologous signal peptides resulted in high levels of secreted expression. The fungal host-expression system combination was tested successfully for the expression of the recombinant therapeutic protein-human interferon beta (HuIFN beta). (C) 2017 Elsevier Ltd. All rights reserved.