Unraveling the Stability of Halophilic Protease Enzymes: A Computational Study

Halophiles thrive in high salt concentrations, requiring more than 0.2 M NaCl for growth and resisting osmotic stress. They are classified based on their salinity concentration, i.e., slight (0.2-0.85 M or 2-5% of NaCl), moderate (0.85-3.4 M or 5-20%  of NaCl), and extreme (3.4-5.1 M or 20-30% of NaCl) Halophiles. The number of acidic residues appears to be balanced by a reduced number of basic residues on a genome-wide scale. The main variance in the composition of halophiles and mesophiles was mainly attributed to the abundance of aspartic acid, lysine, etc. Therefore, discovering more amino acids can lead to new prospects for industrial applications. As Halophilic organisms producing the enzyme protease are being significantly used in detergent, pharmaceutical, and food manufacturing industries, this analysis can further lead to Genome sequencing, mutational studies, protein engineering, etc. Many bioinformatics approaches for proteases, such as PoPS, PROSPER, and PAL, have been used to identify the desired functional properties. Future studies on mutational stability and improving these halophilic proteases' stability can be rationalized through bioinformatics approaches.