 The study focused on identifying and optimizing the serine protease gene f-gapped 4 from fusarium graminorum 2697. This gene was then cloned into the yeast pitchia pastoris to produce the recombinant protein. The protein was found to have high activity and stability over a broad range of temperatures and pH levels. Additionally, it was shown to be compatible with detergents. To further increase the enzyme's activity, a combination of molecular docking and evolutionary analysis was used to identify potential hotspots within the protein structure. Mutation of these hotspots resulted in a more active enzyme, which was named FGAPT4M3. The mutated enzyme was found to have higher activity and catalytic efficiency than the original enzyme, resulting in a more efficient detergent. This article was authored by Xiaowang, Xingqin, Li Geytong, and others.