Purification and characterization of a halotolerant and thermotolerant lipase produced from a novel bacteria "brevibacterium halotolerans PS4 |KX671556|" and its application in detergent formulations

Abstract

An extracellular lipase was isolated and purified from the culture broth of Brevibacterium halotolerans PS4 to provide homogeneity, using ammonium sulfate precipitation, followed by chromatographic techniques on Sephadex G-75 column, resulting in a purification factor of 2.98 fold with specific activity of 1016.10 IU/mg. The molecular weight of the purified lipase was estimated by SDS-PAGE to be 80 kDa. The purified lipase had maximal activity within the pH range of 6 to 7, with an optimum pH of 7, and within the temperature range of 35 to 55°C. The purified lipase exhibited not only stable but enhanced maximal activity by Triton X100. The enzyme activity of Brevibacterium halotolerans PS4 lipase was enhanced by Ca2+ and Mg2+. SDS and metal ions such as Hg2+, Zn2+, Cu2+, Ag2+ and Fe2+ decreased the lipase activity remarkably. The extracellular lipase from orchard soil isolate was further applied for its application as laundry additives.