Optimization, purification, and biochemical characterization of thermoalkaliphilic lipase from a novel Geobacillus stearothermophilus FMR12 for detergent formulations.

This study was aimed to produce a high compatible thermoalkaliphilic lipase (TA) with detergents from new thermophilic bacterial strains utilizing fish wastes for industrial application. Among bacterial isolates, a new Geobacillus stearothermophilus FMR12 efficiently utilized fish wastes at a concentration of 20% (w/v), exhibiting highly lipolytic activity at extreme thermal and alkaline pH conditions. Optimized fermentation parameters of TA lipase production were ascertained, promoting the productivity of the TA lipase from 424 to 1038 U/ml. Purification results of TA lipase exposed prominent specific activity of 4788 U/mg, purification fold of 12.44, and 7.8% yield. The purified TA lipase demonstrated outstanding activity and stability in a temperature range of 40-95 °C and pH (4-11), revealing optimal activity at 70 °C and pH 9. The molecular weight of the enzyme was estimated to be 63 kDa. Compared to control, the TA lipase activity was promoted in the presence of calcium chloride. Likewise, Triton X-100 enhanced the activity of the TA lipase, recording 128% of the control enzyme. Interestingly, the TA lipase conserved higher than 90% of its activity after blending with commercial detergents, emphasizing its competence for detergent formulations.