Process Biochemistry, Vol.77, 159-163, 2019
Extraction and spray drying of Class II hydrophobin HFBI produced by Trichoderma reesei
Hydrophobins are considered the strongest surface-active proteins from microbial origin. The amphiphilic proteins are produced by filamentous fungi and exhibit unique physicochemical properties. Self-assembly into membranes at hydrophobic-hydrophilic interfaces illustrate their unique properties, leading to a broad range of applications, from foam stabilization to protein immobilization. Due to insufficient production quantities of Class II hydrophobins using native fungal strains and limited long-term storage stability of liquid formulations, commercial availability remains lacking. Within this research, the potential of trehalose for stabilization and preservation of hydrophobins during spray drying was studied. Therefore, the Class II hydrophobin HFBI, expressed by Trichoderma reesei, was produced by submerged cultures in fed-batch mode and extracted from the mycelium. Extracts purified with FPLC were subsequently spray dried. Residual activity of 93.62 +/- 5.07% was obtained with trehalose in a ratio of 2:1 (excipient:protein) to stabilize HFBI during spay drying, which demonstrates the huge potential of trehalose.