Journal of Bioscience and Bioengineering, Vol.94, No.6, 530-535, 2002
Recent studies of protein secretion by filamentous fungi
Filamentous fungi have been widely exploited for the homologous and heterologous protein production, because of the high capacity of their protein secretion machinery. However, the production of heterologous proteins is often limited while the production of homologous proteins can be very high. Various researches have reported the methods for overcoming this problem and some techniques, such as the fusion gene system, improve the production of heterologous proteins. Recently, the molecular biological study of solid-state culture attracts the attention, because the long history of biological studies has shown that the productivity of protein in the solid-state culture frequently exceeds the productivity of protein in the submerged culture. The recent researches of solid-state culture have revealed the new aspects of protein production in filamentous fungi. Solid-state specific gene expression was observed in the glaB and pepA genes of Aspergillus oryzae. A GC-box and HSE element of the glaB promoter region affected solid-state specific gene expression of this gene. Solid-state culture-specific release of enzymes from the cell wall was also observed in the production of beta-glucosidases in Aspergillus kawachii. Extracellular soluble polysaccharide (ESP) from A. kawachii was concerned with the location of beta-glucosidases. Moreover, ESP and the cell wall fraction of A. kawachii were shown to be involved in the stability of beta-glucosidases. The knowledge of the molecular biology of solid-state culture should provide new approaches for the production of both homologous and heterologous proteins in both submerged culture and solid-state culture of filamentous fungi.