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Characterization of partially purified alkaline protease secreted by halophilic bacterium Citricoccus sp. isolated from agricultural soil of northern India
- Verma, Jyoti, Pandey, Sangeeta
- Biocatalysis and agricultural biotechnology 2019 v.17 pp. 605-612
- agricultural soils, bacteria, calcium, copper, detergents, enzyme activity, industry, magnesium, pH, research institutions, ribosomal RNA, sequence analysis, serine proteinases, sodium, tea, temperature, India
- The present study reports the isolation of protease producing bacteria Bact2 from agricultural soil of Regional Centre of Soil Salinity Research Institute, Lucknow, India. It was identified as Citricoccus sp. (KC522120.1) by 16S rRNA gene sequencing. The optimum pH and temperature for maximum enzyme production was observed to be at 10 and 40 °C respectively. The enzyme protease was partially purified and recovery of enzyme was 77.16%. A 1.66 fold increase in enzyme activity was also observed in comparison to original. After purification, the partially purified enzyme (PPE) was characterized. The optimum pH and temperature of partially purified enzyme (PPE) activity was observed to be at 10 and 40 °C respectively. The activity of PPE was enhanced in presence of Ca2+ and Mg2+ while it was inhibited by Cu++ and Na+. The PPE was completely inhibited by Phenyl methyl sulphonyl fluoride (PMSF) indicating that it belongs to serine protease group. Finally, enzyme was found to be compatible with detergents and effective in removing stains of tea and ink indicating it's application in detergent industry. Besides, to our knowledge till date production of alkaline protease from Citricoccus sp. has been reported first time in the present manuscript.