Introduction: Vital catalysts have long been widely used in the food industry, but with new applications in many industries, such as the chemical industry, they have become even more important. In biocatalysis, all parts of the cell, cell extract, purified enzyme, inactive cell, or inactive enzymes are used as catalysts in various processes. Enzymes are essential for various industrial, pharmaceutical, and especially biotechnological processes. Keratinase is produced by various microorganisms in the presence of keratin as a substrate. It mainly targets disulfide bonds. In this study, the biochemical properties of keratinase enzymes derived from Bacillus mojavensis (B. mojavensis) were investigated.
Materials and methods: The 3D structure of keratinases from B. mojavensis was created using Modeler software, and the model's validation and refinement indicators, including Prosa, Z-score, and Ramachandran Graph confirmed the high quality of the modeled protein. The PMSF, Pepstatin and leupeptin structures were prepared from the PubChem database server and introduced to the MVD software along with the 3D structure of the keratinase for molecular docking.
Results: The binding energies (Eaint#) for the Mojavensis-PMSF, Mojavensis-Pepstatin and Mojavensis-Leupeptin complexes were -71.73, -334.1 and -211.2, respectively. In all three Mojavensis-PMSF, Mojavensis-Pepstatin and Mojavensis-Leupeptin complexes, the Serine 277 keratinase mojavensis formed a hydrogen bond with inhibitors. Serine 295 also interacted with inhibitors in both of Pepstatin and Leupeptin complexes. Glutamic 299 keratinase mojavensis also interacted with PMSF and Leupeptin. All three PMSF, Pepstatin and leupeptin peptidase inhibitors were able to interact with keratinase mojavensis.
Conclusion: Docking results showed that Serine amino acids 277 and 295 in the active site of keratinase mojavensis, may play a key role in its catalytic function.