Multi-substrate sequential optimization, characterization and immobilization of lipase produced by Pseudomonas plecoglossicida S7

Lipases are important biocatalysts having the third largest global demand after amylases and proteases. In the present study, we have screened 56 potential lipolytic Pseudomonas strains for their lipolytic activity. Pseudomonas plecoglossicida S7 showed highest lipase production with specific activity of 70 U/mg. Statistical optimizations using Plackett Burman design and response surface methodology evaluated fourteen different media supplements including various oilcakes, carbon sources, nitrogen sources, and metal ions which led to a 2.23-fold (156.23 U/mg) increase in lipase activity. Further, inoculum size optimization increased the overall lipase activity by 2.81-folds. The lipase was active over a range of 30–50° C with a pH range (7–10). The enzyme was tolerant to various solvents like chloroform, methanol, 1-butanol, acetonitrile, and dichloromethane and retained 60% of its activity in the presence of sodium dodecyl sulfate (0.5% w/v). The enzyme was immobilized onto Ca-alginate beads which increased thermal (20–60 °C) and pH stability (5–10). The purified enzyme could successfully remove sesame oil stains and degraded upto 25.2% of diesel contaminated soil. These properties of the lipase will help in its applicability in detergent formulations, wastewater treatments, and biodegradation of oil in the environment.