Abstract:Hydrophobin is a class of small molecular weight proteins that have surface stability and can be self-assembled at the interface to form an amphiphilic protein membrane, thus changing the hydrophobicity of the interface. Previous research has shown that hydrophobin is non-toxic and immunogenic, can be used for material surface modification, food surface plasticity, drug target transport or biosensor signal accurate identification. In recent years, a small molecule secretion-type hydrophobin BslA (formerly YuaB) has been found in the biofilm of Bacillus subtilis. The research has shown that the Bacillus subtilis hydrophobin BslA has high expression yield, simple purification process, easy operation and large-scale production, so BslA has greater application advantage and development value. In this review, we summarize the information on the properties, functions and structure of BslA, and compare and analyze them with fungal hydrophobin, and systematically analyze their structural characteristics and application value.