Ahmed_2025_Int.J.Biol.Macromol__144883

This research aimed to optimize, purify, and biochemically and structurally characterize an acid-stable and organic solvent-tolerant lipase from the fungus Monascus pilosus. Sequence alignment indicated that the fungus in this study exhibits a high similarity of 99.63 % with M. pilosus (NR 163510.1). Maximum lipase production (434.3 U/mL) was observed at pH 3 after five days of incubation at 30 degreesC. The structure analysis showed that the lipase belongs to the GXSXL family, and the Ser163, Asp224, and His250 residues construct the catalytic triad. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) estimated the molecular weight of lipase to be around 51 kDa. Maximum lipase activity was detected at pH 8 and 50 degreesC, recording an activity of 625.3 U/mL. This lipase is remarkably stable across a pH range of 1.5 to 9, with a 1.8-fold activity enhancement after 2-h of incubation at pH 1.5. The enzyme displayed considerable stability in chloroform, hexane, toluene, and dimethyl sulfoxide (DMSO), retaining over 85 % residual activity at a 10 % concentration. This novel acid and organic solvent-tolerant lipase can provide a sustainable solution for industrial detergent formulation and other environmentally friendly applications. This is the first report to isolate, purify, and characterize lipase from the genus Monascus.