Production, purification, and characterization of cold-active lipase from the psychrotroph Pseudomonas sp. A6

Abstract

Cold-active lipases are presently employed extensively in the detergent, chemical intermediate, fine chemical, food, and pharmaceutical industries. Seven cold-adaptive bacteria were isolated from the Mediterranean Sea near Alexandria, Egypt, and tested for their ability to produce cold-active lipase, with the highest activity at 10 °C. The most potent isolate was Pseudomonas sp. A6. To determine the most important variables, the bacterium was exposed to a necessary medium component and environmental factor screening using a single factor-at-a-time approach, followed by a multifactorial Plackett-Burman design strategy. After purification and characterization, the optimal activity levels for the cold-active lipase were figured out. Inoculation of Pseudomonas A6 under near optimum conditions using medium consisting of (g/L) peptone 7.14; soybean oil 7.5% (v/v); K2HPO4, 0.4; MgSO4, 0.1; glucose 2; pH 8; and temperature 10 °C led to a maximum lipase activity anticipated to be 23.36 U/mL. Purified lipase showed the best activity and thermal stability at a pH of 8 and a temperature of 10 °C. The Pseudomonas A6 lipase tolerated the monovalent ions, while greater valence ions did not.

Thermostable CaCO3-Immobilized Bacillus subtilis Lipase for Sustainable Biodiesel Production from Waste Cooking Oil

“…This result is in line with those obtained previously [37]. Other lipases showed a curve with an upward trend even after 20 min of incubation time, which continued to increase as the incubation period increased [38].…”

Identification and Characterization of a Novel Thermostable GDSL Lipase LipGt6 from Geobacillus thermoleovorans H9

“…Some of the most commercially important bacteria that produce lipases are Bacillus sp., Pseudomonas sp., and Burkholderia sp. [5][6][7]. These microbial lipases operate at a wider temperature range, and their stability and activity are greater.…”