| Autor: |
Jamal GA; Faculty of Allied Health Sciences, Kuwait University, Kuwait City, Kuwait., Jahangirian E; Department of Molecular, Zist Tashkhis Farda Company (tBioDx), Tehran, Iran., Hamblin MR; Wellman Center for Photomedicine, Massachusetts General Hospital, Harvard Medical School, Boston, MA, USA.; Laser Research Center, Faculty of Health Science, University of Johannesburg, Doornfontein, South Africa., Shirali M; Senior Quantitative Geneticist and Project leader, Agri-Food and Biosciences Institute, Hillsborough, UK and Assistant professor, School of Biological Sciences, Queen's University Belfast, Belfast, UK., Mirzaei H; Research Center for Biochemistry and Nutrition in Metabolic Diseases, Institute for Basic Sciences, Kashan University of Medical Sciences, Kashan, Iran., Tarrahimofrad H; Department of Molecular, Zist Tashkhis Farda Company (tBioDx), Tehran, Iran. |
| Abstrakt: |
One of the major categories of industrial enzymes, proteases is crucial to the survival of living things. The purpose of this research was to newly thermostable protease from the thermophilum Geobacillus stearothermophilus . With the conserved catalytic tetrad, protease (Protease JJ) is closely related to the serine proteases from the subtilisin S8 peptidase, according to phylogenetic tree analysis. The tertiary structure of Protease JJ was predicted structurally using RoseTTAFold, and it is a sandwich structure overall. Homology modeling validation showed Protease JJ was modeled in X-ray's protein areas, and it has gained a favored Ramachandran graph regarding Phi/Psi angels. Protease JJ showed structure stability through Molecular dynamics simulation in the presence of Tween20 and Methanol in 1% concentration. Also, Protease JJ exhibited thermal stability at 60 to 90 °C so that amino acid exposure of Protease JJ was low and constant throughout the MD simulation. Docking results of Protease JJ with BSA and βcasein were simulated via MD and it was found that Protease JJ could interact with both BSA and βcasein strongly. MM/PBSA analysis showed Protease JJ may be involved via more amino acids with BSA as well as established more interaction hydrogen bonds. Overall, evidence suggests Protease JJ probably has merit for future experimental investigation as a thermostable protease.Communicated by Ramaswamy H. Sarma. |
