Bioinformatic analysis of a halophilic protease from moderately halophilic bacterium Nesterenkonia sp. F.

Halophilic enzymes may be useful for harsh condition in industrial processes, especially food industries. Proteases have broad application in industries such as laundry detergents, food processing, and the leather industry. Two third of all industrial enzymes are protease. In this work, one protease from Nestrenkonia sp. strain F has been selected and characterized by some bioinformatic softwares such as SingalP 4.0, GC plot, 3DLigandsite, Protparam, and NCBI blast. Based on analysis of the selected protease, it is predicted that it has 1530 base pair, 47.25% GC content, 509 amino acid, 19% alpha-helix, 17% beta-sheet, 3% TM helix, and signal peptides. It is transmembrane and estimated weight is 53kD and half life in Escherichia coli is less than 20 hours. Homology search revealed homology between protease from Nestrenkonia sp strain F and d1r6va . Nucleotid and amino acid sequences of the selected protease were similar to ‘Kocuria flava strain HO-9041’ and ‘peptidase8 from Micrococcaceae’ respectively. Accordingly, selected protease from Nestrenkonia sp. F. Can be used in many harsh industrial processes when concentrated solution would inhibit many enzymatic convergent.