Biochemical and in-silico structural assessments of an acinetobacter haemolyticus lipase KV1 isolated from an oil palm mill effluent

The use of microbial enzymes as biocatalysts for a myriad of commercial processes are currently trending owing to their versatility and, their use is considerably greener than the chemically-assisted methods. In this regard, this study reports the comprehensive biochemical characterization of a lipase from novel Acinetobacter haemolyticus KV1 bacteria. The intracellular lipase was purified to ~3.5-fold using consecutive treatments of ammonium sulfate precipitation, dialysis and DEAE-cellulose ion exchange chromatography. The purified lipase exhibited maximum relative activity at 40°C and pH 8.0, respectively. Lipase KV1 was significantly activated (p 50% for up to 24 h for pH between pH 7-11. Therefore, the full characterization of lipase KV1 reported in this study deserves scientific and economic considerations