Dynamics of Phylogenetic Diversity and its influence on the production of Extracellular Protease by moderately Halotolerant Alkaliphilic Bacteria Acinetobacter baumannii GTCR407 Nov.

New characters emerge in the population of microorganisms living in the extreme environments due to its adaptation to ecological association. The microorganisms living in saline habitat utilize complex nutrients by adopting different strategies in Deoxyribonucleic Acid (DNA) and Ribonucleic Acid (RNA), which are related to their metabolic and ecological diversities. Isolation and characterization of the organisms producing extracellular protease from such environment were the prime focus of this investigation, which can indicate the importance of metabolic diversity in phylogeny. Norberg medium was used to isolate halotolerant microorganisms from salt-cured skin. The isolates were screened for high activity of protease and the strain showing maximum activity of protease was taken for further studies. The biochemical characterization and 16s ribosomal RNA sequencing studies confirm that the isolate is Acinetobacter baumannii. Moreover, hydrolysis positive for starch and casein, negative for gelatin shows that the organism is a variant form of A. baumannii. Cell growth parameters such as pH and temperature were optimized and their values are 8 and 37oC respectively. The extracellular production of protease was optimized in the suitable medium and its enzyme activity was 165μg/ml/min. The results imply that the isolate had acquired operational genes through lateral gene transfer (LGT) probably from unrelated species in the environment. This indicates that the isolate identified possesses metabolic and ecological diversities with values of phylogenetic delineation

Studies on Industrially Significant Haloalkaline Protease from Bacillus sp. JSGT Isolated from Decaying Skin of Tannery

Eight bacterial strains were isolated from collagen layer of decaying skin sample. Three isolates exhibited the prominent zones of clearance on skim milk agar medium at pH 9.5. These isolates were then characterized and identified. One of the haloalkalophilic isolates belonged to the genus Bacillus. Maximum enzyme activity (228.29 ± 1.89 PU/ ml) was found at pH 9 and temperature 37°C in the strain which is designated as Bacillus sp. JSGT. Basic properties such as effects of different temperature, pH, metal ions and inhibitors on protease activity were also studied. Maximum activity was obtained at pH 9 at 55°C. Ca+2 and Mg+2 ions were found to enhance the relative enzyme activity up to 158 and 136% respectively. However, the activity of protease was completely inhibited by phenyl methyl sulfonyl fluoride (PMSF) that showed its serine nature. The results indicated that enzyme produced by Bacillus sp. JSGT is active within broad ranges of temperature and pH. These characteristics render its potential use in leather and detergent industries