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Cost-Effective Purification and Characterization of an Industrially Important Alkaline Protease from a Newly Isolated Strain of Bacillus sp. ICTF2
- Kaur, Narinder, Gat, Yogesh, Panghal, Anil
- Industrial biotechnology 2019 v.15 no.1 pp. 20-24
- Bacillus (bacteria), biotechnology, calcium, cost effectiveness, detergents, laundry, pH, pharmaceutical industry, proteinases, serine, temperature
- A novel alkaline protease from Bacillus sp. ICTF2 was purified with high efficiency, enhanced activity of 147.9%, and 12-fold purity using three-phase partitioning (TPP), a fast-developing, efficient bioseparation strategy. The purified enzyme retained 96% activity at 40°C, even after 2-h incubation, with pH and optimal temperature of 8 and 40°C, respectively. The enzyme was strongly inhibited by phenylmethylsulfonyl fluoride (PMSF), which demonstrates that the purified alkaline protease belongs to the serine family. Furthermore, the enzyme was highly compatible in various detergents even without the addition of Ca²⁺ and retained more than 75% of its activity in all the detergents. The remarkable properties of the enzyme, such as stability at neutral pH and milder temperature indicate its possible use in food and pharma industries. However, compatibility with many detergents assures that it can potentially be used in the detergent and laundry industries.